Enzyme - Knowledge

1996: 2334: 3288: 2720: 1470: 3608: 3646: 1776: 2308: 1361: 40: 9189: 4420: 1258: 2709: 796: 624: 4269: 1688: 9310: 4283: 3315:. In a metabolic pathway, one enzyme takes the product of another enzyme as a substrate. After the catalytic reaction, the product is then passed on to another enzyme. Sometimes more than one enzyme can catalyze the same reaction in parallel; this can allow more complex regulation: with, for example, a low constant activity provided by one enzyme but an inducible high activity from a second enzyme. 3793:). In addition, MAP is metal-ion dependent while creatinase is not, hence this property was also lost over time. Small changes of enzymatic activity are extremely common among enzymes. In particular, substrate binding specificity (see above) can easily and quickly change with single amino acid changes in their substrate binding pockets. This is frequently seen in the main enzyme classes such as 97: 2371:. The major contribution of Michaelis and Menten was to think of enzyme reactions in two stages. In the first, the substrate binds reversibly to the enzyme, forming the enzyme-substrate complex. This is sometimes called the Michaelis–Menten complex in their honor. The enzyme then catalyzes the chemical step in the reaction and releases the product. This work was further developed by 2390:. To find the maximum speed of an enzymatic reaction, the substrate concentration is increased until a constant rate of product formation is seen. This is shown in the saturation curve on the right. Saturation happens because, as substrate concentration increases, more and more of the free enzyme is converted into the substrate-bound ES complex. At the maximum reaction rate ( 3352:, because the amount of the end product produced is regulated by its own concentration. Negative feedback mechanism can effectively adjust the rate of synthesis of intermediate metabolites according to the demands of the cells. This helps with effective allocations of materials and energy economy, and it prevents the excess manufacture of end products. Like other 875: 3671:, any malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a genetic disease. The malfunction of just one type of enzyme out of the thousands of types present in the human body can be fatal. An example of a fatal genetic disease due to enzyme insufficiency is 2457:

specificity constant is called the diffusion limit and is about 10 to 10 (M s). At this point every collision of the enzyme with its substrate will result in catalysis, and the rate of product formation is not limited by the reaction rate but by the diffusion rate. Enzymes with this property are called

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to tetrahydrofolate. The similarity between the structures of dihydrofolate and this drug are shown in the accompanying figure. This type of inhibition can be overcome with high substrate concentration. In some cases, the inhibitor can bind to a site other than the binding-site of the usual substrate

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which then decays into products. Enzymes increase reaction rates by lowering the energy of the transition state. First, binding forms a low energy enzyme-substrate complex (ES). Second, the enzyme stabilises the transition state such that it requires less energy to achieve compared to the uncatalyzed

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also changes shape slightly as it enters the active site. The active site continues to change until the substrate is completely bound, at which point the final shape and charge distribution is determined. Induced fit may enhance the fidelity of molecular recognition in the presence of competition and

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for all steps in the reaction up to and including the first irreversible step. Because the specificity constant reflects both affinity and catalytic ability, it is useful for comparing different enzymes against each other, or the same enzyme with different substrates. The theoretical maximum for the

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Allosteric sites are pockets on the enzyme, distinct from the active site, that bind to molecules in the cellular environment. These molecules then cause a change in the conformation or dynamics of the enzyme that is transduced to the active site and thus affects the reaction rate of the enzyme. In

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suggested a modification to the lock and key model: since enzymes are rather flexible structures, the active site is continuously reshaped by interactions with the substrate as the substrate interacts with the enzyme. As a result, the substrate does not simply bind to a rigid active site; the amino

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proposed that both the enzyme and the substrate possess specific complementary geometric shapes that fit exactly into one another. This is often referred to as "the lock and key" model. This early model explains enzyme specificity, but fails to explain the stabilization of the transition state that

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is a process where the enzyme is sequestered away from its substrate. Enzymes can be sequestered to the plasma membrane away from a substrate in the nucleus or cytosol. Or within the membrane, an enzyme can be sequestered into lipid rafts away from its substrate in the disordered region. When the

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by other molecules. For example, the end product(s) of a metabolic pathway are often inhibitors for one of the first enzymes of the pathway (usually the first irreversible step, called committed step), thus regulating the amount of end product made by the pathways. Such a regulatory mechanism is

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reflect sequence similarity. For instance, two ligases of the same EC number that catalyze exactly the same reaction can have completely different sequences. Independent of their function, enzymes, like any other proteins, have been classified by their sequence similarity into numerous families.

1131:. Each enzyme is described by "EC" followed by a sequence of four numbers which represent the hierarchy of enzymatic activity (from very general to very specific). That is, the first number broadly classifies the enzyme based on its mechanism while the other digits add more and more specificity. 3694:, result in build-up of phenylalanine and related products. Some mutations are in the active site, directly disrupting binding and catalysis, but many are far from the active site and reduce activity by destabilising the protein structure, or affecting correct oligomerisation. This can lead to 3318:

Enzymes determine what steps occur in these pathways. Without enzymes, metabolism would neither progress through the same steps and could not be regulated to serve the needs of the cell. Most central metabolic pathways are regulated at a few key steps, typically through enzymes whose activity

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mechanism. If an enzyme produces too much of one substance in the organism, that substance may act as an inhibitor for the enzyme at the beginning of the pathway that produces it, causing production of the substance to slow down or stop when there is sufficient amount. This is a form of

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catalyzes a reaction in a first step and then checks that the product is correct in a second step. This two-step process results in average error rates of less than 1 error in 100 million reactions in high-fidelity mammalian polymerases. Similar proofreading mechanisms are also found in

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enzyme is released it mixes with its substrate. Alternatively, the enzyme can be sequestered near its substrate to activate the enzyme. For example, the enzyme can be soluble and upon activation bind to a lipid in the plasma membrane and then act upon molecules in the plasma membrane.

1295:) when heated or exposed to chemical denaturants and this disruption to the structure typically causes a loss of activity. Enzyme denaturation is normally linked to temperatures above a species' normal level; as a result, enzymes from bacteria living in volcanic environments such as 1971:

Since coenzymes are chemically changed as a consequence of enzyme action, it is useful to consider coenzymes to be a special class of substrates, or second substrates, which are common to many different enzymes. For example, about 1000 enzymes are known to use the coenzyme NADH.

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contained within the yeast cells called "ferments", which were thought to function only within living organisms. He wrote that "alcoholic fermentation is an act correlated with the life and organization of the yeast cells, not with the death or putrefaction of the cells."

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cannot bind to the free enzyme, only to the enzyme-substrate complex; hence, these types of inhibitors are most effective at high substrate concentration. In the presence of the inhibitor, the enzyme-substrate complex is inactive. This type of inhibition is rare.

1291:. The sequence of the amino acids specifies the structure which in turn determines the catalytic activity of the enzyme. Although structure determines function, a novel enzymatic activity cannot yet be predicted from structure alone. Enzyme structures unfold ( 2011:, which then decays into lower-energy products. When enzyme catalysed (solid line), the enzyme binds the substrates (ES), then stabilizes the transition state (ES) to reduce the activation energy required to produce products (EP) which are finally released. 2289:

Enzymes can couple two or more reactions, so that a thermodynamically favorable reaction can be used to "drive" a thermodynamically unfavourable one so that the combined energy of the products is lower than the substrates. For example, the hydrolysis of

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binds to an allosteric site and the binding of the substrate and the inhibitor affect each other. The enzyme's function is reduced but not eliminated when bound to the inhibitor. This type of inhibitor does not follow the Michaelis–Menten equation.

4776:(Translation: In order to obviate misunderstandings and avoid cumbersome periphrases, suggests designating as "enzymes" the unformed or not organized ferments, whose action can occur without the presence of organisms and outside of the same.) 4770:"Um Missverständnissen vorzubeugen und lästige Umschreibungen zu vermeiden schlägt Vortragender vor, die ungeformten oder nicht organisirten Fermente, deren Wirkung ohne Anwesenheit von Organismen und ausserhalb derselben erfolgen kann, als 2029:

As with all catalysts, enzymes do not alter the position of the chemical equilibrium of the reaction. In the presence of an enzyme, the reaction runs in the same direction as it would without the enzyme, just more quickly. For example,

3544:) which in turn affects enzyme activity. In contrast to partitioning into membrane bound organelles, enzyme subcellular localisation may also be altered through polymerisation of enzymes into macromolecular cytoplasmic filaments. 1858:, which uses a zinc cofactor bound as part of its active site. These tightly bound ions or molecules are usually found in the active site and are involved in catalysis. For example, flavin and heme cofactors are often involved in 3259:, respectively) into smaller ones, so they can be absorbed by the intestines. Starch molecules, for example, are too large to be absorbed from the intestine, but enzymes hydrolyze the starch chains into smaller molecules such as 6530:

Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, et al. (February 2005). "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II".

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Enzymes are not rigid, static structures; instead they have complex internal dynamic motions – that is, movements of parts of the enzyme's structure such as individual amino acid residues, groups of residues forming a

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and other industrial applications when extremely specific catalysts are required. Enzymes in general are limited in the number of reactions they have evolved to catalyze and also by their lack of stability in

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Since inhibitors modulate the function of enzymes they are often used as drugs. Many such drugs are reversible competitive inhibitors that resemble the enzyme's native substrate, similar to

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Bar-Even A, Noor E, Savir Y, Liebermeister W, Davidi D, Tawfik DS, Milo R (May 2011). "The moderately efficient enzyme: evolutionary and physicochemical trends shaping enzyme parameters".

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The biochemical identity of enzymes was still unknown in the early 1900s. Many scientists observed that enzymatic activity was associated with proteins, but others (such as Nobel laureate

2250: 2130: 2545: 3765:. A key question is therefore whether and how enzymes can change their enzymatic activities alongside. It is generally accepted that many new enzyme activities have evolved through 982:, he found that sugar was fermented by yeast extracts even when there were no living yeast cells in the mixture. He named the enzyme that brought about the fermentation of sucrose " 5792:"Um ein Bild zu gebrauchen, will ich sagen, dass Enzym und Glucosid wie Schloss und Schlüssel zu einander passen müssen, um eine chemische Wirkung auf einander ausüben zu können." 4980:

Blake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR (May 1965). "Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution".

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this way, allosteric interactions can either inhibit or activate enzymes. Allosteric interactions with metabolites upstream or downstream in an enzyme's metabolic pathway cause

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where it is activated. This stops the enzyme from digesting the pancreas or other tissues before it enters the gut. This type of inactive precursor to an enzyme is known as a

2678: 3702:, in which the body's ability to break down choline ester drugs is impaired. Oral administration of enzymes can be used to treat some functional enzyme deficiencies, such as 1811:

Some enzymes do not need additional components to show full activity. Others require non-protein molecules called cofactors to be bound for activity. Cofactors can be either

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Renugopalakrishnan V, Garduño-Juárez R, Narasimhan G, Verma CS, Wei X, Li P (November 2005). "Rational design of thermally stable proteins: relevance to bionanotechnology".

1462:, having broad specificity and acting on a range of different physiologically relevant substrates. Many enzymes possess small side activities which arose fortuitously (i.e. 1314:. Only a small portion of their structure (around 2–4 amino acids) is directly involved in catalysis: the catalytic site. This catalytic site is located next to one or more 2580: 1249:

may spread these genes to unrelated species, especially bacteria where they can replace endogenous genes of the same function, leading to hon-homologous gene displacement.

1987:. This continuous regeneration means that small amounts of coenzymes can be used very intensively. For example, the human body turns over its own weight in ATP each day. 1893:

Coenzymes are small organic molecules that can be loosely or tightly bound to an enzyme. Coenzymes transport chemical groups from one enzyme to another. Examples include

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and mutation of the duplicate copies although evolution can also happen without duplication. One example of an enzyme that has changed its activity is the ancestor of

1835:). These cofactors serve many purposes; for instance, metal ions can help in stabilizing nucleophilic species within the active site. Organic cofactors can be either 1120: 1975:

Coenzymes are usually continuously regenerated and their concentrations maintained at a steady level inside the cell. For example, NADPH is regenerated through the

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Enzyme kinetics is the investigation of how enzymes bind substrates and turn them into products. The rate data used in kinetic analyses are commonly obtained from

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evolution. These efforts have begun to be successful, and a few enzymes have now been designed "from scratch" to catalyze reactions that do not occur in nature.

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As enzymes are made up of proteins, their actions are sensitive to change in many physio chemical factors such as pH, temperature, substrate concentration, etc.

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and substrate cannot bind to the enzyme at the same time. Often competitive inhibitors strongly resemble the real substrate of the enzyme. For example, the drug

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is only one of several important kinetic parameters. The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the

1666:. Different states within this ensemble may be associated with different aspects of an enzyme's function. For example, different conformations of the enzyme 1299:

are prized by industrial users for their ability to function at high temperatures, allowing enzyme-catalysed reactions to be operated at a very high rate.

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for "his discovery of cell-free fermentation". Following Buchner's example, enzymes are usually named according to the reaction they carry out: the suffix

5794:(To use an image, I will say that an enzyme and a glucoside must fit like a lock and key, in order to be able to exert a chemical effect on each other.) 2733:(right) are very similar in structure (differences show in green). As a result, methotrexate is a competitive inhibitor of many enzymes that use folates. 2417:), which is the substrate concentration required for an enzyme to reach one-half its maximum reaction rate; generally, each enzyme has a characteristic 7230:

Fisher JF, Meroueh SO, Mobashery S (February 2005). "Bacterial resistance to beta-lactam antibiotics: compelling opportunism, compelling opportunity".

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Ramanathan A, Savol A, Burger V, Chennubhotla CS, Agarwal PK (January 2014). "Protein conformational populations and functionally relevant substates".

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Chapman-Smith A, Cronan JE (September 1999). "The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity".

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that make up the active site are molded into the precise positions that enable the enzyme to perform its catalytic function. In some cases, such as

5465: 5292: 4787: 1220:(EC 2.7.1.1) is a transferase (EC 2) that adds a phosphate group (EC 2.7) to a hexose sugar, a molecule containing an alcohol group (EC 2.7.1). 4519:"BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA" 655: 8999: 8898: 2691:

and thermodynamically driven random collision. Many biochemical or cellular processes deviate significantly from these conditions, because of

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Flatmark T, Stevens RC (August 1999). "Structural Insight into the Aromatic Amino Acid Hydroxylases and Their Disease-Related Mutant Forms".

7403:"Infrared evidence of cyanide binding to iron and copper sites in bovine heart cytochrome c oxidase. Implications regarding oxygen reduction" 2397:) of the enzyme, all the enzyme active sites are bound to substrate, and the amount of ES complex is the same as the total amount of enzyme. 2495:. The turnover of such enzymes can reach several million reactions per second. But most enzymes are far from perfect: the average values of 7146:(July 1986). "Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides". 1670:

are associated with the substrate binding, catalysis, cofactor release, and product release steps of the catalytic cycle, consistent with

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recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their

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of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules:

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Artificial (in vitro) evolution is now commonly used to modify enzyme activity or specificity for industrial applications (see below).

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is reduced. In contrast to competitive inhibition, non-competitive inhibition cannot be overcome with high substrate concentration.

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In some enzymes, no amino acids are directly involved in catalysis; instead, the enzyme contains sites to bind and orient catalytic

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is an active area of research and involves attempts to create new enzymes with novel properties, either through rational design or

3575:) available for metabolic reactions. This provides a mechanism for regulating the overall metabolism of the organism. For example, 17: 4866:

The naming of enzymes by adding the suffix "-ase" to the substrate on which the enzyme acts, has been traced to French scientist

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Enzymes must bind their substrates before they can catalyse any chemical reaction. Enzymes are usually very specific as to what

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Rodnina MV, Wintermeyer W (2001). "Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms".

5448: 5140: 1322:. The remaining majority of the enzyme structure serves to maintain the precise orientation and dynamics of the active site. 811:. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is 5935:(2nd ed.). New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. pp. 137–8. 427: 8154:

Okada S, O'Brien JS (August 1969). "Tay-Sachs disease: generalized absence of a beta-D-N-acetylhexosaminidase component".

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Distorting bound substrate(s) into their transition state form to reduce the energy required to reach the transition state

8826:"Improved performances and control of beer fermentation using encapsulated alpha-acetolactate decarboxylase and modeling" 3436:

of enzyme genes) can be enhanced or diminished by a cell in response to changes in the cell's environment. This form of

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Guzmán-Maldonado H, Paredes-López O (September 1995). "Amylolytic enzymes and products derived from starch: a review".

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and constrained molecular movement. More recent, complex extensions of the model attempt to correct for these effects.

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Farris PL (2009). "Economic Growth and Organization of the U.S. Starch Industry". In BeMiller JN, Whistler RL (eds.).

4699:[Memoir on diastase, the principal products of its reactions, and their applications to the industrial arts]. 1096:. An enzyme's name is often derived from its substrate or the chemical reaction it catalyzes, with the word ending in 9452: 9214: 9178: 9135: 7009: 6738: 6713: 6578: 5940: 5821: 5477: 4799: 4410: 1940: 1894: 1727: 60: 1582:

Creating an environment with a charge distribution complementary to that of the transition state to lower its energy

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characteristics to the substrates. Enzymes can therefore distinguish between very similar substrate molecules to be

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Wlodawer A, Vondrasek J (1998). "Inhibitors of HIV-1 protease: a major success of structure-assisted drug design".

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Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MH (August 2006). "Electrostatic basis for enzyme catalysis".

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binds to a site other than where the substrate binds. The substrate still binds with its usual affinity and hence K

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Temporarily reacting with the substrate, forming a covalent intermediate to provide a lower energy transition state

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via a series of intermediate metabolites. Each chemical modification (red box) is performed by a different enzyme.

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Alkorta I, Garbisu C, Llama MJ, Serra JL (January 1998). "Industrial applications of pectic enzymes: a review".

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fashion because the enzymes from the unaffected genes are generally sufficient to prevent symptoms in carriers.

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and closely related compounds (vitamins) must be acquired from the diet. The chemical groups carried include:

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Ochoa D, Bradley D, Beltrao P (February 2018). "Evolution, dynamics and dysregulation of kinase signalling".

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Enzymes are usually much larger than their substrates. Sizes range from just 62 amino acid residues, for the

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Michaelis L, Menten M (1913). "Die Kinetik der Invertinwirkung" [The Kinetics of Invertase Action].

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is an irreversible enzyme inhibitor that combines with the copper and iron in the active site of the enzyme

9337: 7976:"Identification of novel filament-forming proteins in Saccharomyces cerevisiae and Drosophila melanogaster" 2459: 1307: 5158:"Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution" 1910: 1651: 1546: 1292: 1266: 844: 608: 553: 482: 3721:

enzymes. Defects in these enzymes cause cancer because cells are less able to repair mutations in their

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involves the hydrolysis of ATP. Because this reaction releases so much energy, other reactions that are

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where residues orient the substrates. The catalytic site and binding site together compose the enzyme's

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These families have been documented in dozens of different protein and protein family databases such as

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Sun Y, Cheng J (May 2002). "Hydrolysis of lignocellulosic materials for ethanol production: a review".

6345:"Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms" 3983: 3356:, the control of enzymatic action helps to maintain a stable internal environment in living organisms. 2789: 1671: 1074:

and published in 1965. This high-resolution structure of lysozyme marked the beginning of the field of

412: 8115:"Familial hyperglycemia due to mutations in glucokinase. Definition of a subtype of diabetes mellitus" 3645: 2646: 950: 9709: 9696: 9683: 9670: 9657: 9644: 9631: 9593: 8653:

Jiang L, Althoff EA, Clemente FR, Doyle L, Röthlisberger D, Zanghellini A, et al. (March 2008).

4164: 3777:) which are clearly homologous but catalyze very different reactions (MAP removes the amino-terminal 3687: 3612: 2020: 1976: 1663: 1448: 1087: 1058:

The discovery that enzymes could be crystallized eventually allowed their structures to be solved by

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Zenkin N, Yuzenkova Y, Severinov K (July 2006). "Transcript-assisted transcriptional proofreading".

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Jaeger KE, Eggert T (August 2004). "Enantioselective biocatalysis optimized by directed evolution".

4419: 1208:: catalyze the movement of ions or molecules across membranes, or their separation within membranes. 978:

submitted his first paper on the study of yeast extracts in 1897. In a series of experiments at the

9603: 9557: 9500: 9314: 9007: 8906: 8315: 4081: 3770: 3703: 3429: 2550: 2468: 1396: 1246: 1128: 1040: 997: 987: 392: 8930:"Review: Compounds Involved in the Flavor of Surface Mold-Ripened Cheeses: Origins and Properties" 7949:

Suzuki H (2015). "Chapter 4: Effect of pH, Temperature, and High Pressure on Enzymatic Activity".

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Khersonsky O, Tawfik DS (2010). "Enzyme promiscuity: a mechanistic and evolutionary perspective".

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for an enzyme reaction showing the relation between the substrate concentration and reaction rate.

9505: 9330: 8074:"Structural basis for allosteric regulation of the monomeric allosteric enzyme human glucokinase" 7906:"Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling" 3695: 3592: 3465: 2809: 2768: 2692: 1843:, which are tightly bound to an enzyme. Organic prosthetic groups can be covalently bound (e.g., 1820: 1806: 1705: 1698: 1667: 1659: 1562: 1528: 1426:

Some of the enzymes showing the highest specificity and accuracy are involved in the copying and

1326: 519: 457: 122: 117: 63: 7659:"Recent advances in rumen microbial ecology and metabolism: potential impact on nutrient output" 5769: 5320:

Chen LH, Kenyon GL, Curtin F, Harayama S, Bembenek ME, Hajipour G, Whitman CP (September 1992).

4470:"A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties" 4433:

Murphy JM, Farhan H, Eyers PA (April 2017). "Bio-Zombie: the rise of pseudoenzymes in biology".

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remains the same. However the inhibitor reduces the catalytic efficiency of the enzyme so that V

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for glucose yet is more sensitive to glucose concentration. This enzyme is involved in sensing

3433: 3400:. Another example of post-translational modification is the cleavage of the polypeptide chain. 3185: 2835: 2291: 1946: 1914: 1902: 1885:; here the holoenzyme is the complete complex containing all the subunits needed for activity. 1780: 1740: 1478: 1435: 1071: 944: 558: 472: 422: 5100:. School of Biological and Chemical Sciences, Queen Mary, University of London. Archived from 4755: 1348:

exist, which again can act alone or in complex with proteins. The most common of these is the

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Murzin AG (November 1993). "Can homologous proteins evolve different enzymatic activities?".

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Johnson LN, Petsko GA (July 1999). "David Phillips and the origin of structural enzymology".

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Enzyme changes shape by induced fit upon substrate binding to form enzyme-substrate complex.

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Begley CG, Paragina S, Sporn A (March 1990). "An analysis of contact lens enzyme cleaners".

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can be coupled to ATP hydrolysis, driving the overall series of linked metabolic reactions.

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reaction (ES). Finally the enzyme-product complex (EP) dissociates to release the products.

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catalyzes its reaction in either direction depending on the concentration of its reactants:

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Enzymes can be compartmentalized, with different metabolic pathways occurring in different

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in 1937. The conclusion that pure proteins can be enzymes was definitively demonstrated by

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Manchester KL (December 1995). "Louis Pasteur (1822–1895)--chance and the prepared mind".

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Schomburg I, Chang A, Placzek S, Söhngen C, Rother M, Lang M, et al. (January 2013).

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Murphy JM, Zhang Q, Young SN, Reese ML, Bailey FP, Eyers PA, et al. (January 2014).

3824: 3707: 3624: 3169: 2887: 2364: 2322: 1647: 1311: 910: 724: 603: 526: 402: 177: 30:"Biocatalyst" redirects here. For the use of natural catalysts in organic chemistry, see 8726: 8670: 8450: 8167: 8113:

Froguel P, Zouali H, Vionnet N, Velho G, Vaxillaire M, Sun F, et al. (March 1993).

6955: 6683:(3rd ed.). Baltimore, Maryland: Lippincott Williams & Wilkins. pp. 312–3. 6633: 6405: 6269: 6244: 6201: 6121: 5981: 5854: 5584: 5322:"4-Oxalocrotonate tautomerase, an enzyme composed of 62 amino acid residues per monomer" 5220: 5132: 4993: 4579: 9741: 9495: 9404: 9394: 9081: 8855: 8687: 8654: 8618:

Hult K, Berglund P (August 2003). "Engineered enzymes for improved organic synthesis".

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Cleaver JE (May 1968). "Defective repair replication of DNA in xeroderma pigmentosum".

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Changeux JP, Edelstein SJ (June 2005). "Allosteric mechanisms of signal transduction".

6369: 6344: 6282: 6141: 6000: 5965: 5604: 5553: 5392: 5184: 5157: 5013: 4599: 4543: 4518: 4494: 4469: 4296: 4160: 3861: 3809: 3201: 3189: 3165: 2684: 2472: 2031: 1855: 1459: 1213: 1075: 789: 712: 538: 9042: 8772: 8734: 8631: 7856: 7831: 7599: 7574: 7419: 7402: 7335: 7318: 6920: 6508: 5909: 5873: 5838: 5745: 5728: 5338: 5321: 5044: 4932: 4915: 4731: 3607: 1070:

that digests the coating of some bacteria; the structure was solved by a group led by

9280: 9254: 9210: 9174: 9167: 9131: 9108: 9073: 8978: 8878: 8847: 8804: 8776: 8738: 8692: 8635: 8600: 8565: 8530: 8526: 8493: 8462: 8419: 8370: 8279: 8244: 8179: 8136: 8095: 8054: 8005: 7954: 7931: 7884: 7879:

Skett P, Gibson GG (2001). "Chapter 3: Induction and Inhibition of Drug Metabolism".

7861: 7812: 7761: 7731: 7680: 7639: 7604: 7555: 7550: 7525: 7498: 7493: 7476: 7457: 7447: 7424: 7375: 7371: 7340: 7299: 7247: 7212: 7163: 7159: 7117: 7113: 7075: 7038: 7005: 6967: 6924: 6889: 6854: 6805: 6744: 6734: 6709: 6684: 6657: 6574: 6548: 6512: 6475: 6417: 6374: 6325: 6317: 6274: 6225: 6220: 6185: 6164: 6133: 6088: 6065: 6028: 6005: 5946: 5936: 5913: 5878: 5817: 5750: 5709: 5674: 5670: 5639: 5635: 5596: 5545: 5510: 5473: 5444: 5384: 5343: 5300: 5273: 5232: 5189: 5136: 5048: 5005: 4937: 4795: 4735: 4634: 4591: 4548: 4499: 4450: 4406: 4306: 4191: 4140: 3815: 3742: 3714: 3633: 3521: 3481: 3389: 3349: 3312: 3292: 3267:, which can then be absorbed. Different enzymes digest different food substances. In 3240: 2868: 2864: 2278: 2016: 2004: 2000: 1927: 1840: 1793: 1764: 1572: 1568: 1491: 1466:), which may be the starting point for the evolutionary selection of a new function. 1463: 1420: 1378: 1365: 1278: 1212:

These sections are subdivided by other features such as the substrate, products, and

855: 808: 777:

an enzyme, but even in the decades since ribozymes' discovery in 1980-1982, the word

740: 504: 447: 442: 437: 372: 68: 9085: 8859: 7510: 7387: 7175: 6979: 6429: 5608: 5557: 5396: 2435:, which is the number of substrate molecules handled by one active site per second. 9731: 9541: 9536: 9510: 9438: 9065: 9038: 8970: 8941: 8837: 8768: 8730: 8682: 8674: 8627: 8592: 8557: 8522: 8474: 8454: 8409: 8401: 8360: 8350: 8271: 8236: 8227:

Erlandsen H, Stevens RC (October 1999). "The structural basis of phenylketonuria".

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De Clercq E (April 2002). "Highlights in the development of new antiviral agents".

7594: 7590: 7586: 7545: 7537: 7488: 7414: 7367: 7330: 7289: 7281: 7270:"Strategies for discovering and derisking covalent, irreversible enzyme inhibitors" 7239: 7202: 7155: 7129: 7109: 7065: 7034: 6959: 6916: 6881: 6844: 6836: 6795: 6787: 6647: 6637: 6540: 6504: 6409: 6364: 6356: 6309: 6286: 6264: 6256: 6215: 6205: 6145: 6125: 6108:

Benkovic SJ, Hammes-Schiffer S (August 2003). "A perspective on enzyme catalysis".

6057: 5995: 5985: 5905: 5868: 5858: 5781: 5740: 5701: 5666: 5631: 5588: 5537: 5502: 5414: 5374: 5333: 5263: 5224: 5179: 5169: 5128: 5040: 5017: 4997: 4927: 4903: 4727: 4626: 4603: 4583: 4538: 4530: 4489: 4481: 4442: 4048: 3965: 3766: 3662: 3564: 3473: 3441: 3405: 3344: 3340: 3205: 2822: 2741: 2376: 2360: 2314: 2282: 2133: 2008: 1995: 1918: 1881:

can also be applied to enzymes that contain multiple protein subunits, such as the

1824: 1640: 1558: 1416: 1412: 1341: 1284: 1270: 1154: 1019:) argued that proteins were merely carriers for the true enzymes and that proteins 835:

are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal

824: 820: 736: 674: 514: 432: 407: 8759:

Kirk O, Borchert TV, Fuglsang CC (August 2002). "Industrial enzyme applications".

8040: 7070: 7053: 6963: 6907:

Ellis RJ (October 2001). "Macromolecular crowding: obvious but underappreciated".

4898:

Willstätter R (1927). "Faraday lecture. Problems and methods in enzyme research".

4867: 934: 9588: 9572: 9485: 9206:

New Beer in an Old Bottle: Eduard Buchner and the Growth of Biochemical Knowledge

8175: 6776:"The original Michaelis constant: translation of the 1913 Michaelis-Menten paper" 5990: 5506: 5228: 5207:

Anfinsen CB (July 1973). "Principles that govern the folding of protein chains".

4877: 4630: 4617:

Callahan BP, Miller BG (December 2007). "OMP decarboxylase--An enigma persists".

4301: 4168: 4065: 3820: 3730: 3683: 3616: 3568: 3560: 3509: 3469: 3385: 3369: 2350: 1620: 1601:

By orienting the substrates into a productive arrangement to reduce the reaction

1427: 1330: 1288: 1024: 854:. Some household products use enzymes to speed up chemical reactions: enzymes in 847:

when exposed to excessive heat, losing their structure and catalytic properties.

743:

depend upon enzymes to catalyze individual steps. The study of enzymes is called

477: 149: 9056:

Bajpai P (March 1999). "Application of enzymes in the pulp and paper industry".

8131: 8114: 5379: 5362: 4758:[On the behavior of various organized and so-called unformed ferments]. 9626: 9567: 9353: 8582: 8304:. Bethesda (MD): National Center for Biotechnology Information (US). 1998–2015. 8297: 7716: 6622:

Proceedings of the National Academy of Sciences of the United States of America

6190:

Proceedings of the National Academy of Sciences of the United States of America

5843:

Proceedings of the National Academy of Sciences of the United States of America

4400: 4274: 4113: 3726: 3676: 3453: 3373: 3287: 2907: 2903: 1882: 1655: 1444: 1439: 1139: 1109: 1009: 975: 898:

were known but the mechanisms by which these occurred had not been identified.

732: 543: 452: 397: 8974: 8561: 8390:"Lactose malabsorption and intolerance: pathogenesis, diagnosis and treatment" 8090: 8073: 6260: 5805: 5268: 5251: 3517: 2746:

Enzyme reaction rates can be decreased by various types of enzyme inhibitors.

2708: 2488: 939: 781:

alone often means the protein type specifically (as is used in this article).

9725: 9531: 9490: 9374: 9364: 8405: 8339:"Enzyme replacement therapy for pancreatic insufficiency: present and future" 7635: 7461: 7207: 7190: 6748: 6210: 5931:

Boyer R (2002). "Chapter 6: Enzymes I, Reactions, Kinetics, and Inhibition".

5785: 4874:– the first enzyme to be isolated – by introducing this practice in his book 4756:"Über das Verhalten verschiedener organisirter und sog. ungeformter Fermente" 4210: 4187: 3951: 3691: 3620: 3553: 3513: 3377: 3233: 3221: 2915: 2839: 2453: 2387: 1784: 1624: 1373: 1198: 922: 902: 804: 462: 335: 276: 259: 254: 212: 199: 8678: 6642: 6413: 6129: 5950: 5592: 5067: 4587: 1873:. An enzyme together with the cofactor(s) required for activity is called a 1605:

change (the contribution of this mechanism to catalysis is relatively small)

1216:. An enzyme is fully specified by four numerical designations. For example, 1078:

and the effort to understand how enzymes work at an atomic level of detail.

866:

break down proteins into smaller molecules, making the meat easier to chew.

9480: 9369: 9220: 9077: 8851: 8780: 8742: 8696: 8639: 8604: 8569: 8423: 8374: 8283: 8248: 8240: 8099: 8058: 8009: 7816: 7735: 7643: 7559: 7303: 7251: 7216: 7121: 7079: 6971: 6928: 6893: 6858: 6809: 6661: 6552: 6516: 6421: 6378: 6329: 6278: 6229: 6184:

Villa J, Strajbl M, Glennon TM, Sham YY, Chu ZT, Warshel A (October 2000).

6137: 6069: 6009: 5917: 5882: 5754: 5713: 5678: 5643: 5600: 5549: 5514: 5277: 5193: 5174: 5052: 4941: 4638: 4552: 4503: 4454: 4222: 3653:

fashion because there are more non-X chromosomes than X-chromosomes, and a

3401: 3193: 2911: 2875: 2764: 2730: 2719: 2367:

proposed a quantitative theory of enzyme kinetics, which is referred to as

2356: 2333: 1839:, which are released from the enzyme's active site during the reaction, or 1828: 1537: 1315: 1241:. Unrelated enzymes that have the same enzymatic activity have been called 1124: 1052: 758:

Enzymes are known to catalyze more than 5,000 biochemical reaction types.

748: 723:, and the enzyme converts the substrates into different molecules known as 573: 568: 531: 509: 377: 88: 31: 9112: 8982: 8534: 8466: 8388:

Misselwitz B, Pohl D, Frühauf H, Fried M, Vavricka SR, Fox M (June 2013).

8183: 8140: 7991: 7935: 7883:(3 ed.). Cheltenham, UK: Nelson Thornes Publishers. pp. 87–118. 7865: 7684: 7608: 7502: 7428: 7379: 7344: 7167: 5388: 5363:"The animal fatty acid synthase: one gene, one polypeptide, seven enzymes" 5347: 5236: 5009: 4739: 4595: 4534: 3460:

within the penicillin molecule. Another example comes from enzymes in the

2898:. A common example of an irreversible inhibitor that is used as a drug is 795: 9704: 9639: 9475: 8596: 7847: 7541: 5863: 5810: 4907: 4288: 4131: 4052: 3969: 3903:

Remove protein, starch, and fat or oil stains from laundry and dishware.

3738: 3668: 3596: 3584: 3525: 3457: 3397: 3353: 3331:

There are five main ways that enzyme activity is controlled in the cell.

3320: 3272: 3177: 2883: 1611:

Enzymes may use several of these mechanisms simultaneously. For example,

1567:

Enzymes can accelerate reactions in several ways, all of which lower the

1469: 1408: 1404: 1319: 1205: 1150: 1055:. These three scientists were awarded the 1946 Nobel Prize in Chemistry. 926: 836: 316: 294: 289: 284: 264: 237: 232: 139: 56: 44: 4446: 1775: 1112:. Different enzymes that catalyze the same chemical reaction are called 9185:, A biochemistry textbook available free online through NCBI Bookshelf. 8875:

Ingredients in Meat Products Properties, Functionality and Applications

8355: 7191:"A Perspective on the Kinetics of Covalent and Irreversible Inhibition" 6733:(Third, enlarged and improved ed.). Weinheim, Germany: Wiley-VCH. 5896:

Vasella A, Davies GJ, Böhm M (October 2002). "Glycosidase mechanisms".

4485: 4201: 4154: 4150: 4010: 3778: 3774: 3762: 3758: 3718: 3580: 3576: 3497: 3477: 3449: 3296: 3209: 2891: 2843: 2772: 2726: 1958: 1952: 1712: in this section. Unsourced material may be challenged and removed. 1662:

of slightly different structures that interconvert with one another at

1628: 1533: 1474: 1296: 1217: 1169: 1090:

similarity (and thus evolutionary relationship) or enzymatic activity.

1031:

was a pure protein and crystallized it; he did likewise for the enzyme

957: 851: 752: 728: 583: 249: 217: 172: 154: 9069: 8842: 8825: 8275: 7917: 7798: 7285: 7243: 6885: 6840: 6791: 6544: 6321: 6313: 6061: 5127:. Chichester, UK: John Wiley & Sons, Ltd. pp. a0003058.pub2. 3637: 1797: 1501: 1495: 1382: 72: 9678: 9652: 9389: 8458: 6360: 5729:"Catalytic promiscuity and the evolution of new enzymatic activities" 5001: 4760:

Verhandlungen des Naturhistorisch-medicinischen Vereins zu Heidelberg

4681:

Volume IV: Modern Development of the Chemical and Biological Sciences

4125: 4121: 4056: 4030: 3933: 3908: 3869: 3855: 3786: 3556: 3541: 3537: 3529: 3476:. Enzyme levels can also be regulated by changing the rate of enzyme 3276: 3229: 3213: 2688: 2307: 1865:

Enzymes that require a cofactor but do not have one bound are called

1812: 1486: 1183: 1165: 1143: 1067: 972:

was used to refer to chemical activity produced by living organisms.

850:

Some enzymes are used commercially, for example, in the synthesis of

716: 39: 5839:"Application of a Theory of Enzyme Specificity to Protein Synthesis" 5098:

International Union of Biochemistry and Molecular Biology (NC-IUBMB)

4948: 3512:

and used by a different set of enzymes as a source of energy in the

2452:. This is also called the specificity constant and incorporates the 2206: 2086: 1687: 1403:

is achieved by binding pockets with complementary shape, charge and

6447:. International Union of Pure and Applied Chemistry. Archived from 5541: 4871: 4268: 4216: 4183: 4146: 4089: 4025: 3990: 3937: 3914: 3890: 3782: 3754: 3588: 3533: 3409: 3393: 3304: 3268: 3248: 2859: 2484: 2480: 1836: 1760: 1612: 1541: 1452: 1369: 1360: 1349: 1345: 1179:: cleave various bonds by means other than hydrolysis and oxidation 1063: 1032: 906: 766: 762: 708: 578: 308: 269: 207: 5806:"Chapter 2.2: The Central Role of Enzymes as Biological Catalysts" 3860:

Break down cellulose into sugars that can be fermented to produce

3725:. This causes a slow accumulation of mutations and results in the 2379:, who derived kinetic equations that are still widely used today. 9414: 9409: 9322: 8205: 8072:

Kamata K, Mitsuya M, Nishimura T, Eiki J, Nagata Y (March 2004).

6299: 4338: 4247: 4237: 4107: 4099: 4071: 3999: 3929: 3923: 3894: 3875: 3849: 3572: 3524:

of the enzyme to different compartments may change the degree of

3501: 3417: 3413: 3381: 3300: 3264: 3260: 3256: 3244: 2919: 2899: 2847: 1936: 1922: 1763:

regulation, altering the activity of the enzyme according to the

1616: 1602: 1303: 1113: 1101: 1048: 1005: 1001: 914: 704: 52: 48: 6594: 6474:. Hoboken, New Jersey: John Wiley & Sons, Inc. p. 336. 4808: 3311:

Several enzymes can work together in a specific order, creating

874: 9691: 9309: 7319:"The discovery and development of HMG-CoA reductase inhibitors" 7025:

Price NC (1979). "What is meant by 'competitive inhibition'?".

6186:"How important are entropic contributions to enzyme catalysis?" 5772:[Influence of configuration on the action of enzymes]. 4956:"Nobel Prizes and Laureates: The Nobel Prize in Chemistry 1946" 4566:

Radzicka A, Wolfenden R (January 1995). "A proficient enzyme".

4328: 4323: 4318: 4243: 4231: 4197: 4077: 4042: 4034: 4005: 3898: 3794: 3753:

Similar to any other protein, enzymes change over time through

3722: 3252: 3197: 3181: 3173: 2918:. Other enzyme inhibitors are poisons. For example, the poison 2879: 1844: 1482: 1477:

has a large induced fit motion that closes over the substrates

1431: 1194: 1187: 1044: 1028: 983: 965: 895: 887: 863: 832: 224: 6871: 5528:

Shevelev IV, Hübscher U (May 2002). "The 3' 5' exonucleases".

3208:. Enzymes are also involved in more exotic functions, such as 1623:, stabilize charge build-up on the transition states using an 1257: 9665: 9419: 9399: 8960: 6774:

Michaelis L, Menten ML, Johnson KA, Goody RS (October 2011).

5156:

Omelchenko MV, Galperin MY, Wolf YI, Koonin EV (April 2010).

4177: 4095: 4019: 3713:

Another way enzyme malfunctions can cause disease comes from

3461: 3217: 1859: 1176: 918: 891: 6445:"Glossary of Terms Used in Bioinorganic Chemistry: Cofactor" 5155: 4516: 4282: 3682:

One example of enzyme deficiency is the most common type of

3667:

Since the tight control of enzyme activity is essential for

3649:

Hereditary defects in enzymes are generally inherited in an

3615:

over 300 different mutations throughout the structure cause

1352:

which is a complex of protein and catalytic RNA components.

882:

By the late 17th and early 18th centuries, the digestion of

96: 6773: 6529: 6087:(6th ed.). New York, N.Y.: W.H. Freeman. p. 195. 6083:

Cox MM, Nelson DL (2013). "Chapter 6.2: How enzymes work".

5123:

Mulder NJ (28 September 2007). "Protein Family Databases".

4333: 3975: 3957: 3943: 3790: 3686:. Many different single amino acid mutations in the enzyme 3628: 2253: 1832: 1232: 992: 883: 828: 689: 680: 340: 9430: 8823: 8492:(11th ed.). London: Saunders/ Elsevier. p. 567. 8387: 8071: 7756:

Suzuki H (2015). "Chapter 8: Control of Enzyme Activity".

6942:

Kopelman R (September 1988). "Fractal reaction kinetics".

3220:

can also contain enzymes for infecting cells, such as the

3192:, and also transport cargo around the cell as part of the 1372:

example. Binding sites in blue, catalytic site in red and

8652: 8112: 7832:"Molecular basis of beta-lactamase induction in bacteria" 6615: 5072:

International Union of Biochemistry and Molecular Biology

3279:, to break down the cellulose cell walls of plant fiber. 3275:

diets, microorganisms in the gut produce another enzyme,

2941:

The following table shows pH optima for various enzymes.

2895: 2838:

permanently inactivates the enzyme, usually by forming a

2438:

The efficiency of an enzyme can be expressed in terms of

2238: 2225: 2195: 2177: 2118: 2105: 2075: 2057: 1816: 1121:

International Union of Biochemistry and Molecular Biology

859: 9028: 6703: 5774:

Berichte der Deutschen Chemischen Gesellschaft zu Berlin

5570: 5319: 4842:"Eduard Buchner – Nobel Lecture: Cell-Free Fermentation" 3404:, a digestive protease, is produced in inactive form as 1514:

To explain the observed specificity of enzymes, in 1894

964:

was used later to refer to nonliving substances such as

739:

in order to occur at rates fast enough to sustain life.

7974:

Noree C, Sato BK, Broyer RM, Wilhelm JE (August 2010).

7783:"GSK-3: tricks of the trade for a multi-tasking kinase" 7267: 6183: 6107: 5770:"Einfluss der Configuration auf die Wirkung der Enzyme" 5413:. The European Bioinformatics Institute. Archived from 3690:, which catalyzes the first step in the degradation of 3571:

and therefore have different sets of enzymes (known as

1086:

Enzymes can be classified by two main criteria: either

840: 827:

are molecules that increase activity. Many therapeutic

8029:

Critical Reviews in Biochemistry and Molecular Biology

7973: 7360:

Annual Review of Biophysics and Biomolecular Structure

7229: 6995: 6993: 6991: 6989: 6047: 5472:(3rd ed.). Weinheim: Wiley-VCH. pp. 89–114. 4870:(1840–1904), who intended to honor the discoverers of 2003:. Uncatalysed (dashed line), substrates need a lot of 1261:

Enzyme activity initially increases with temperature (

8655:"De novo computational design of retro-aldol enzymes" 7700:"Cyclooxygenases: structural and functional insights" 5439:

Suzuki H (2015). "Chapter 7: Active Site Structure".

4879:

Traité de microbiologie: Diastases, toxines et venins

4792:

The Oxford Companion to the History of Modern Science

4655:(1752). "Observations sur la digestion des oiseaux". 4467: 3757:

and sequence divergence. Given their central role in

3472:. Induction or inhibition of these enzymes can cause 2649: 2588: 2553: 2501: 2165: 2045: 695: 686: 683: 8758: 8336: 6595:"BRENDA The Comprehensive Enzyme Information System" 5726: 4979: 4264: 3168:

inside living organisms. They are indispensable for

2933: 1925:. These coenzymes cannot be synthesized by the body 1854:

An example of an enzyme that contains a cofactor is

1399:

they bind and then the chemical reaction catalysed.

755:

sequences and unusual 'pseudocatalytic' properties.

9098: 8547: 8490:

Andrews' Diseases of the Skin: Clinical Dermatology

6986: 6494: 6342: 5622:Ibba M, Soll D (2000). "Aminoacyl-tRNA synthesis". 4884:

Microbiology Treatise: diastases, toxins and venoms

2858:In many organisms, inhibitors may act as part of a 692: 677: 9166: 9164: 5809: 5656: 5470:Biochemistry of Signal Transduction and Regulation 5091: 4398: 3359: 2672: 2636:{\displaystyle 10^{5}{\rm {s}}^{-1}{\rm {M}}^{-1}} 2635: 2574: 2539: 2424:for a given substrate. Another useful constant is 2244: 2124: 1081: 909:, in 1833. A few decades later, when studying the 8824:Dulieu C, Moll M, Boudrant J, Poncelet D (2000). 8487: 7872: 7357: 7268:Johnson DS, Weerapana E, Cravatt BF (June 2010). 6674: 6616:Törnroth-Horsefield S, Neutze R (December 2008). 6391: 5895: 4565: 4432: 3913:Remove food stains from the common food additive 2294:is often used to drive other chemical reactions. 1509: 1485:. Binding sites in blue, substrates in black and 925:concluded that this fermentation was caused by a 823:are molecules that decrease enzyme activity, and 59:residues in red, maltose substrate in black, and 27:Large biological molecule that acts as a catalyst 9723: 8927: 8226: 8153: 7903: 7751: 7749: 7747: 7745: 7575:"Molecular biology of bacterial bioluminescence" 7523: 7400: 7092: 7045: 6999: 6101: 5691: 5527: 5434: 5432: 4891: 4886:] (in French). Paris, France: Masson and Co. 4794:. Oxford: Oxford University Press. p. 270. 3698:if the disease is untreated. Another example is 3392:, helps control the synthesis or degradation of 2687:, which is derived from the assumptions of free 1787:. Thiamine pyrophosphate cofactor in yellow and 960:, in yeast', to describe this process. The word 8994: 8992: 8261: 8208:. U.S. National Human Genome Research Institute 8025:"Metabolic regulation via enzyme filamentation" 6761: 5443:. Boca Raton, FL: CRC Press. pp. 117–140. 5249: 2780:to change the shape of the usual binding-site. 1333:where the binding of a small molecule causes a 9274: 9202: 9101:Journal of the American Optometric Association 9006:. European Union. 10 July 2010. Archived from 8963:Critical Reviews in Food Science and Nutrition 8905:. European Union. 10 July 2010. Archived from 7760:. Boca Raton, FL: CRC Press. pp. 141–69. 7142: 7093:Wu P, Clausen MH, Nielsen TE (December 2015). 6677:"Chapter 9: The Pulmonary System and Exercise" 6564: 6562: 6027:. San Francisco: W.H. Freeman. pp. 50–2. 5964:Savir Y, Tlusty T (May 2007). Scalas E (ed.). 4616: 4394: 4392: 4390: 4388: 4386: 4384: 4382: 4380: 4378: 4376: 4374: 2313:A chemical reaction mechanism with or without 1957:formyl, methenyl or methyl groups, carried by 1587:By providing an alternative reaction pathway: 9446: 9338: 9173:(5th ed.). New York, NY: W. H. Freeman. 8220: 7953:. Boca Raton, FL: CRC Press. pp. 53–74. 7942: 7829: 7780: 7742: 7697: 7095:"Allosteric small-molecule kinase inhibitors" 6865: 6822: 6731:Enzyme kinetics : principles and methods 6469: 6343:Tsai CJ, Del Sol A, Nussinov R (March 2009). 5816:(2nd ed.). Washington (DC ): ASM Press. 5429: 5030: 4405:(5th ed.). San Francisco: W.H. Freeman. 4372: 4370: 4368: 4366: 4364: 4362: 4360: 4358: 4356: 4354: 3989:Increase fermentation efficiency by reducing 3500:are synthesized by one set of enzymes in the 3396:and allows the cell to respond to changes in 1595:By destabilizing the substrate ground state: 649: 9251:How Enzymes Work: From Structure to Function 8989: 8617: 7951:How Enzymes Work: From Structure to Function 7758:How Enzymes Work: From Structure to Function 7615: 7524:Berg JS, Powell BC, Cheney RE (April 2001). 6704:Ferguson SJ, Nicholls D, Ferguson S (2002). 6488: 5492: 5441:How Enzymes Work: From Structure to Function 5024: 3823:and at high temperatures. As a consequence, 3781:in new proteins while creatinase hydrolyses 3761:, enzyme evolution plays a critical role in 3228:, or for viral release from cells, like the 886:by stomach secretions and the conversion of 7878: 7823: 7691: 7656: 6559: 6016: 5963: 5797: 5290: 4897: 4694: 4610: 4461: 3487: 3239:An important function of enzymes is in the 2277:The rate of a reaction is dependent on the 2245:{\displaystyle {\ce {CO2{}+H2O<-H2CO3}}} 2125:{\displaystyle {\ce {CO2{}+H2O->H2CO3}}} 9453: 9439: 9345: 9331: 8803:(1st ed.). London: Blackie Academic. 8794: 8792: 8790: 8343:Clinical and Experimental Gastroenterology 7774: 7263: 7261: 7018: 6728: 6442: 6245:"The catalytic triad of serine peptidases" 4717: 4657:Histoire de l'Académie Royale des Sciences 4651: 4645: 4351: 3942:Split polysaccharides and proteins in the 3803: 2853: 2850:are common drugs that act in this manner. 2777: 656: 642: 8945: 8928:Molimard P, Spinnler HE (February 1996). 8841: 8708: 8706: 8686: 8585:Journal of Nanoscience and Nanotechnology 8413: 8364: 8354: 8130: 8089: 8048: 8022: 7999: 7925: 7855: 7806: 7725: 7715: 7674: 7621: 7598: 7549: 7492: 7418: 7334: 7293: 7206: 7069: 7054:"The molecular perspective: methotrexate" 6848: 6825:"A Note on the Kinetics of Enzyme Action" 6799: 6651: 6641: 6618:"Opening and closing the metabolite gate" 6568: 6368: 6268: 6219: 6209: 6158: 6082: 5999: 5989: 5872: 5862: 5803: 5744: 5378: 5337: 5267: 5183: 5173: 4931: 4900:Journal of the Chemical Society (Resumed) 4875: 4542: 4493: 3602: 2878:above; other well-known examples include 2767:is a competitive inhibitor of the enzyme 2540:{\displaystyle k_{\rm {cat}}/K_{\rm {m}}} 1728:Learn how and when to remove this message 1677: 803:Like all catalysts, enzymes increase the 9248: 8754: 8752: 8712: 8481: 8394:United European Gastroenterology Journal 7948: 7755: 7310: 7051: 6941: 6697: 6022: 5836: 5685: 5621: 5463: 5438: 5206: 4673: 3741:in response to even minimal exposure to 3644: 3606: 3286: 2683:Michaelis–Menten kinetics relies on the 1994: 1774: 1747: 1468: 1359: 1265:) until the enzyme's structure unfolds ( 1256: 873: 869: 794: 38: 9165:Berg JM, Tymoczko JL, Stryer L (2002). 8787: 8436: 8337:Fieker A, Philpott J, Armand M (2011). 7572: 7258: 7188: 5767: 5293:"Chapter 1: From sequence to structure" 4916:"So do we understand how enzymes work?" 4559: 4399:Stryer L, Berg JM, Tymoczko JL (2002). 3583:pathway, has a specialized form called 3547: 3456:are induced that hydrolyse the crucial 2867:. Major metabolic pathways such as the 1310:, to over 2,500 residues in the animal 1066:, an enzyme found in tears, saliva and 14: 9724: 9125: 9055: 8798: 8703: 8512: 8488:James WD, Elston D, Berger TG (2011). 7904:Faergeman NJ, Knudsen J (April 1997). 7830:Bennett PM, Chopra I (February 1993). 7474: 7004:(3 ed.). London: Portland Press. 6675:McArdle WD, Katch F, Katch VL (2006). 6242: 5727:O'Brien PJ, Herschlag D (April 1999). 5530:Nature Reviews. Molecular Cell Biology 5122: 4785: 3536:) or oxidative state (e.g., oxidizing 3480:. The opposite of enzyme induction is 3326: 3159: 2749: 1438:" mechanisms. Here, an enzyme such as 1337:that increases or decreases activity. 1043:, who worked on the digestive enzymes 1023:were incapable of catalysis. In 1926, 719:upon which enzymes may act are called 9434: 9326: 9279:(4th ed.). Weinheim: Wiley-VCH. 8872: 8749: 8550:Current Opinion in Structural Biology 7836:Antimicrobial Agents and Chemotherapy 7024: 6906: 6708:(3rd ed.). San Diego: Academic. 6597:. Technische Universität Braunschweig 6161:Catalysis in Chemistry and Enzymology 5930: 5706:10.1146/annurev-biochem-030409-143718 5360: 4753: 4677:A History of Science: in Five Volumes 3960:and beer filtration characteristics. 3773:(MAP) and creatine amidinohydrolase ( 1579:By stabilizing the transition state: 1329:. Enzyme structures may also contain 905:was the first to discover an enzyme, 843:, and many enzymes are (permanently) 9153: 7781:Doble BW, Woodgett JR (April 2003). 7698:Rouzer CA, Marnett LJ (April 2009). 7657:Mackie RI, White BA (October 1990). 7441: 7401:Yoshikawa S, Caughey WS (May 1990). 7316: 6249:Cellular and Molecular Life Sciences 6085:Lehninger Principles of Biochemistry 5466:"The Regulations of Enzyme Activity" 5059: 4913: 3675:, in which patients lack the enzyme 3412:and transported in this form to the 3180:. They also generate movement, with 2156: 2036: 1710:adding citations to reliable sources 1681: 1522: 1390: 1243:non-homologous isofunctional enzymes 1239:Non-homologous isofunctional enzymes 1129:EC numbers (for "Enzyme Commission") 1008:) or to the type of reaction (e.g., 813:orotidine 5'-phosphate decarboxylase 769:. They are sometimes described as a 8877:. New York: Springer. p. 177. 8318:. U.S. National Library of Medicine 8119:The New England Journal of Medicine 7624:Mini Reviews in Medicinal Chemistry 7407:The Journal of Biological Chemistry 5898:Current Opinion in Chemical Biology 5326:The Journal of Biological Chemistry 5299:. London: New Science. p. 27. 5250:Dunaway-Mariano D (November 2008). 5133:10.1002/9780470015902.a0003058.pub2 4752:Kühne coined the word "enzyme" in: 4312: 3599:and regulating insulin production. 3444:. For example, bacteria may become 2771:, which catalyzes the reduction of 1631:using an oriented water substrate. 1619:perform covalent catalysis using a 1344:-based biological catalysts called 24: 9352: 9148: 9130:(3rd ed.). London: Academic. 8206:"Learning About Tay–Sachs Disease" 3737:, which causes the development of 3729:. An example of such a hereditary 3380:. For example, in the response to 2783: 2656: 2619: 2602: 2566: 2563: 2560: 2531: 2514: 2511: 2508: 862:stains on clothes, and enzymes in 25: 9763: 9302: 8947:10.3168/jds.S0022-0302(96)76348-8 8316:"Pseudocholinesterase deficiency" 8229:Molecular Genetics and Metabolism 7676:10.3168/jds.S0022-0302(90)78986-2 6681:Essentials of Exercise Physiology 4888:See Chapter 1, especially page 9. 2934:Factors affecting enzyme activity 1990: 1767:through the rest of the pathway. 1458:Conversely, some enzymes display 1134:The top-level classification is: 996:is combined with the name of the 9308: 9233:, A history of early enzymology. 9187: 9119: 9092: 9049: 9022: 8954: 8921: 8891: 8866: 8817: 8761:Current Opinion in Biotechnology 8646: 8620:Current Opinion in Biotechnology 8611: 8576: 8541: 8506: 8430: 8381: 8330: 8308: 8290: 8255: 7372:10.1146/annurev.biophys.27.1.249 7114:10.1016/j.pharmthera.2015.10.002 6470:Voet D, Voet J, Pratt C (2016). 5671:10.1146/annurev.biochem.70.1.415 5636:10.1146/annurev.biochem.69.1.617 5495:Current Opinion in Biotechnology 5065: 4701:Annales de chimie et de physique 4435:Biochemical Society Transactions 4418: 4281: 4267: 3164:Enzymes serve a wide variety of 2803: 2729:(left) and the anti-cancer drug 2718: 2707: 2673:{\displaystyle 10{\rm {s}}^{-1}} 2332: 2306: 1999:The energies of the stages of a 1945:the phosphate group, carried by 1686: 1190:changes within a single molecule 937:(1837–1900) first used the term 673: 623: 622: 95: 9277:Fundamentals of Enzyme Kinetics 9128:Starch Chemistry and Technology 8198: 8147: 8106: 8065: 8016: 7967: 7897: 7881:Introduction to Drug Metabolism 7650: 7566: 7517: 7468: 7435: 7394: 7351: 7223: 7182: 7136: 7102:Pharmacology & Therapeutics 7086: 7002:Fundamentals of Enzyme Kinetics 6935: 6900: 6816: 6755: 6722: 6668: 6609: 6587: 6523: 6463: 6436: 6385: 6336: 6293: 6236: 6177: 6152: 6076: 6041: 5957: 5924: 5889: 5830: 5761: 5720: 5650: 5615: 5564: 5521: 5486: 5457: 5403: 5354: 5313: 5284: 5243: 5200: 5149: 5116: 5085: 4973: 4860: 4779: 4746: 4711: 3700:pseudocholinesterase deficiency 3388:of multiple enzymes, including 3366:post-translational modification 3360:Post-translational modification 3172:and cell regulation, often via 2829: 1905:(ATP). Some coenzymes, such as 1697:needs additional citations for 1658:. These motions give rise to a 1273:at an intermediate temperature. 1082:Classification and nomenclature 9405:"Minerals" (Chemical elements) 9243:Enzyme structure and mechanism 9203:Cornish-Bowden A, ed. (1997). 8515:Trends in Biochemical Sciences 7591:10.1128/MMBR.55.1.123-142.1991 7446:. New Delhi: S. Chand and Co. 7027:Trends in Biochemical Sciences 6909:Trends in Biochemical Sciences 6823:Briggs GE, Haldane JB (1925). 6497:Trends in Biochemical Sciences 6025:Enzyme Structure and Mechanism 5812:The Cell: a Molecular Approach 5297:Protein structure and function 5033:Trends in Biochemical Sciences 4768:Relevant passage on page 190: 4688: 4667: 4510: 4426: 4033:protein in the manufacture of 3299:releases energy by converting 2754: 2467:. Example of such enzymes are 1985:methionine adenosyltransferase 1434:. Some of these enzymes have " 858:break down protein, starch or 13: 1: 9253:. Boca Raton, FL: CRC Press. 9043:10.1016/S0032-9592(97)00046-0 8773:10.1016/S0958-1669(02)00328-2 8735:10.1016/S0960-8524(01)00212-7 8632:10.1016/S0958-1669(03)00095-8 8041:10.3109/10409238.2016.1172555 7530:Molecular Biology of the Cell 7420:10.1016/S0021-9258(19)39023-4 7336:10.1016/S0022-2275(20)41379-3 7071:10.1634/theoncologist.4-4-340 7052:Goodsell DS (1 August 1999). 6964:10.1126/science.241.4873.1620 6921:10.1016/S0968-0004(01)01938-7 6509:10.1016/s0968-0004(99)01438-3 6302:Accounts of Chemical Research 5910:10.1016/S1367-5931(02)00380-0 5837:Koshland DE (February 1958). 5746:10.1016/S1074-5521(99)80033-7 5694:Annual Review of Biochemistry 5659:Annual Review of Biochemistry 5624:Annual Review of Biochemistry 5339:10.1016/S0021-9258(19)37101-7 5045:10.1016/S0968-0004(99)01423-1 4933:10.1016/S0969-2126(00)00125-8 4732:10.1016/S0167-7799(00)89014-9 4529:(Database issue): D764–D772. 4344: 3334: 3321:thermodynamically unfavorable 3282: 2698: 2575:{\displaystyle k_{\rm {cat}}} 1964:the methyl group, carried by 1951:the acetyl group, carried by 933:In 1877, German physiologist 8527:10.1016/0968-0004(93)90132-7 8176:10.1126/science.165.3894.698 7912:. 323 ( Pt 1) (Pt 1): 1–12. 7526:"A millennial myosin census" 7494:10.1016/0092-8674(95)90405-0 7444:Fundamentals of biochemistry 7160:10.1016/0014-5793(86)81424-7 7039:10.1016/0968-0004(79)90205-6 6472:Fundamentals of Biochemistry 5991:10.1371/journal.pone.0000468 5507:10.1016/j.copbio.2004.06.007 5229:10.1126/science.181.4096.223 4631:10.1016/j.bioorg.2007.07.004 3748: 3251:break down large molecules ( 3243:of animals. Enzymes such as 2871:make use of this mechanism. 1888: 1770: 1552: 1355: 1308:4-oxalocrotonate tautomerase 1287:, acting alone or in larger 1252: 1161:a methyl or phosphate group) 986:". In 1907, he received the 799:IUPAC definition for enzymes 773:of enzyme rather than being 7: 9460: 9209:. Universitat de València. 8132:10.1056/NEJM199303113281005 7980:The Journal of Cell Biology 7189:Strelow JM (January 2017). 5380:10.1096/fasebj.8.15.8001737 5291:Petsko GA, Ringe D (2003). 5252:"Enzyme function discovery" 4695:Payen A, Persoz JF (1833). 4260: 4094:Lower the protein level of 3978:and adjust fermentability. 3587:expressed in the liver and 3567:have different patterns of 3423: 3350:negative feedback mechanism 2297: 2267: 2147: 1911:flavin adenine dinucleotide 1634: 1547:conformational proofreading 1004:is the enzyme that cleaves 790:three-dimensional structure 554:Bioorganometallic chemistry 483:Volume combustion synthesis 10: 9768: 8023:Aughey GN, Liu JL (2015). 7717:10.1194/jlr.R800042-JLR200 7274:Future Medicinal Chemistry 5411:"The Catalytic Site Atlas" 4762:. new series (in German). 4228: 4207: 4174: 4137: 4119: 4105: 4087: 4062: 4040: 4016: 3996: 3984:Acetolactate decarboxylase 3981: 3963: 3949: 3920: 3906: 3881: 3867: 3846: 3807: 3660: 3579:, the first enzyme in the 2739: 2469:triose-phosphate isomerase 2377:J. B. S. Haldane 2348: 2014: 1877:(or haloenzyme). The term 1804: 1751: 1672:catalytic resonance theory 1638: 1556: 1449:aminoacyl tRNA synthetases 1276: 1197:: join two molecules with 1062:. This was first done for 856:biological washing powders 413:Enantioselective synthesis 29: 9617: 9609:Michaelis–Menten kinetics 9581: 9550: 9519: 9468: 9360: 9275:Cornish-Bowden A (2012). 9000:"Protease – GMO Database" 8975:10.1080/10408399509527706 8899:"Chymosin – GMO Database" 8562:10.1016/j.sbi.2017.12.008 8091:10.1016/j.str.2004.02.005 7704:Journal of Lipid Research 7573:Meighen EA (March 1991). 7475:Hunter T (January 1995). 7323:Journal of Lipid Research 7000:Cornish-Bowden A (2004). 6261:10.1007/s00018-005-5160-x 6243:Polgár L (October 2005). 5361:Smith S (December 1994). 5269:10.1016/j.str.2008.10.001 4229: 4165:polymerase chain reaction 4063: 4017: 3921: 3882: 3847: 3688:phenylalanine hydroxylase 3613:phenylalanine hydroxylase 3468:, which are important in 3200:in the cell membrane are 2910:enzymes that produce the 2790:non-competitive inhibitor 2408:Michaelis–Menten constant 2386:conditions and substrate 2369:Michaelis–Menten kinetics 2021:Thermodynamic equilibrium 1977:pentose phosphate pathway 1783:and protein structure of 1269:), leading to an optimal 418:Fully automated synthesis 363:Artificial gene synthesis 9501:Diffusion-limited enzyme 8934:Journal of Dairy Science 8406:10.1177/2050640613484463 7663:Journal of Dairy Science 7636:10.2174/1389557024605474 7317:Endo A (November 1992). 7208:10.1177/1087057116671509 6211:10.1073/pnas.97.22.11899 5933:Concepts in Biochemistry 5786:10.1002/cber.18940270364 5092:Nomenclature Committee. 4820:Nobel Laureate Biography 4790:. In Heilbron JL (ed.). 4082:high-fructose corn syrup 3878:for biofuel production. 3814:Enzymes are used in the 3771:methionyl aminopeptidase 3704:pancreatic insufficiency 3488:Subcellular distribution 3466:cytochrome P450 oxidases 3446:resistant to antibiotics 2816: 1921:(THF), are derived from 1247:Horizontal gene transfer 1041:Wendell Meredith Stanley 988:Nobel Prize in Chemistry 393:Custom peptide synthesis 18:Enzyme-substrate complex 9269:Kinetics and inhibition 8679:10.1126/science.1152692 7910:The Biochemical Journal 7787:Journal of Cell Science 7579:Microbiological Reviews 6829:The Biochemical Journal 6643:10.1073/pnas.0810654106 6414:10.1126/science.1108595 6163:. Mineola, N.Y: Dover. 6130:10.1126/science.1085515 5733:Chemistry & Biology 5593:10.1126/science.1127422 4720:Trends in Biotechnology 4588:10.1126/science.7809611 4474:The Biochemical Journal 4225:to prevent infections. 3804:Industrial applications 3696:intellectual disability 3627:coenzyme in black, and 3452:because enzymes called 3136:Adenosine triphosphate 2854:Functions of inhibitors 2810:uncompetitive inhibitor 2769:dihydrofolate reductase 2693:macromolecular crowding 2382:Enzyme rates depend on 2317:. The enzyme (E) binds 1983:-adenosylmethionine by 1807:Cofactor (biochemistry) 1779:Chemical structure for 1668:dihydrofolate reductase 1660:conformational ensemble 1563:Transition state theory 1027:showed that the enzyme 943:, which comes from 763:catalytic RNA molecules 761:Other biocatalysts are 707:that act as biological 520:Bioorthogonal chemistry 9058:Biotechnology Progress 8830:Biotechnology Progress 8715:Bioresource Technology 8241:10.1006/mgme.1999.2922 6571:Vitamins and Coenzymes 6443:de Bolster MW (1997). 5175:10.1186/1745-6150-5-31 4684:. Harper and Brothers. 4523:Nucleic Acids Research 3727:development of cancers 3658: 3642: 3603:Involvement in disease 3339:Enzymes can be either 3308: 3186:adenosine triphosphate 2836:irreversible inhibitor 2674: 2637: 2576: 2541: 2246: 2126: 2012: 1947:adenosine triphosphate 1915:thiamine pyrophosphate 1903:adenosine triphosphate 1802: 1781:thiamine pyrophosphate 1741:Substrate presentation 1678:Substrate presentation 1506: 1479:adenosine triphosphate 1387: 1283:Enzymes are generally 1274: 1072:David Chilton Phillips 894:by plant extracts and 879: 800: 788:comes from its unique 559:Bioinorganic chemistry 473:Solvothermal synthesis 423:Hydrothermal synthesis 77: 9594:Eadie–Hofstee diagram 9527:Allosteric regulation 9385:Essential fatty acids 9197:Etymology and history 7992:10.1083/jcb.201003001 6729:Bisswanger H (2017). 4914:Blow D (April 2000). 4161:restriction digestion 3735:xeroderma pigmentosum 3648: 3631:cofactor in yellow. ( 3610: 3559:, cells in different 3506:endoplasmic reticulum 3494:cellular compartments 3290: 3226:reverse transcriptase 2902:, which inhibits the 2761:competitive inhibitor 2675: 2638: 2577: 2542: 2460:catalytically perfect 2247: 2127: 1998: 1907:flavin mononucleotide 1791:substrate in black. ( 1778: 1754:Allosteric regulation 1748:Allosteric modulation 1489:cofactor in yellow. ( 1472: 1376:substrate in black. ( 1363: 1335:conformational change 1260: 1106:alcohol dehydrogenase 1060:x-ray crystallography 1012:forms DNA polymers). 877: 870:Etymology and history 798: 749:pseudoenzyme analysis 609:Glossary of chemistry 564:Biophysical chemistry 468:Solid-phase synthesis 322:Amino acid metabolism 300:Nucleotide metabolism 243:Fatty-acid metabolism 42: 9604:Lineweaver–Burk plot 9317:at Wikimedia Commons 9031:Process Biochemistry 8597:10.1166/jnn.2005.441 7848:10.1128/aac.37.2.153 7542:10.1091/mbc.12.4.780 7442:Jain JL (May 1999). 6349:Molecular BioSystems 6255:(19–20): 2161–2172. 5864:10.1073/pnas.44.2.98 5417:on 27 September 2018 4908:10.1039/JR9270001359 4674:Williams HS (1904). 4619:Bioorganic Chemistry 4080:, such as in making 4076:Produce sugars from 3885:Biological detergent 3717:in genes coding for 3548:Organ specialization 3212:generating light in 2993:Lipase (castor oil) 2928:cellular respiration 2924:cytochrome c oxidase 2647: 2586: 2551: 2499: 2493:superoxide dismutase 2477:acetylcholinesterase 2163: 2043: 2025:Chemical equilibrium 1966:S-adenosylmethionine 1939:ion (H), carried by 1849:pyruvate carboxylase 1821:iron–sulfur clusters 1789:xylulose 5-phosphate 1706:improve this article 1654:, or even an entire 1510:"Lock and key" model 1146:/reduction reactions 1037:John Howard Northrop 980:University of Berlin 549:Bioorganic chemistry 388:Convergent synthesis 368:Biomimetic synthesis 190:Biomolecule families 9223:on 13 December 2010 9010:on 24 February 2015 8727:2002BiTec..83....1S 8671:2008Sci...319.1387J 8665:(5868): 1387–1391. 8451:1968Natur.218..652C 8168:1969Sci...165..698O 7793:(Pt 7): 1175–1186. 6956:1988Sci...241.1620K 6950:(4873): 1620–1626. 6634:2008PNAS..10519565T 6628:(50): 19565–19566. 6406:2005Sci...308.1424C 6400:(5727): 1424–1428. 6202:2000PNAS...9711899V 6196:(22): 11899–11904. 6122:2003Sci...301.1196B 6116:(5637): 1196–1202. 5982:2007PLoSO...2..468S 5855:1958PNAS...44...98K 5585:2006Sci...313..518Z 5332:(25): 17716–17721. 5221:1973Sci...181..223A 4994:1965Natur.206..757B 4703:. 2nd (in French). 4580:1995Sci...267...90R 4535:10.1093/nar/gks1049 4447:10.1042/bst20160400 4221:Remove proteins on 3825:protein engineering 3708:lactose intolerance 3625:tetrahydrobiopterin 3528:(e.g., the neutral 3428:Enzyme production ( 3354:homeostatic devices 3327:Control of activity 3170:signal transduction 3160:Biological function 3026:Amylase (pancreas) 2945: 2894:infections such as 2888:protease inhibitors 2882:used to treat high 2750:Types of inhibition 2465:kinetically perfect 2365:Maud Leonora Menten 2281:needed to form the 2240: 2227: 2212: 2197: 2179: 2120: 2107: 2092: 2077: 2059: 1847:in enzymes such as 1652:secondary structure 1312:fatty acid synthase 1226:. EC categories do 1224:Sequence similarity 1088:amino acid sequence 1017:Richard Willstätter 729:metabolic processes 604:Glossary of biology 527:Medicinal chemistry 497:Biochemistry fields 403:Divergent synthesis 178:List of biochemists 167:List of biochemists 83:Part of a series on 47:converts the sugar 9563:Enzyme superfamily 9496:Enzyme promiscuity 8799:Briggs DE (1998). 8356:10.2147/CEG.S17634 8302:Genes and Disease 7710:(Suppl): S29–S34. 6573:. Krieger Pub Co. 6569:Wagner AL (1975). 6451:on 21 January 2017 6159:Jencks WP (1987). 5804:Cooper GM (2000). 5768:Fischer E (1894). 5104:on 1 December 2014 4876:Duclaux E (1899). 4786:Holmes FL (2003). 4486:10.1042/BJ20131174 4297:Industrial enzymes 4192:lignin peroxidases 4013:meat for cooking. 3862:cellulosic ethanol 3810:Industrial enzymes 3715:germline mutations 3659: 3643: 3313:metabolic pathways 3309: 3190:muscle contraction 3188:(ATP) to generate 3004:Lipase (pancreas) 2944: 2685:law of mass action 2670: 2633: 2572: 2537: 2473:carbonic anhydrase 2431:, also called the 2242: 2228: 2215: 2209:Carbonic anhydrase 2185: 2167: 2122: 2108: 2095: 2089:Carbonic anhydrase 2065: 2047: 2032:carbonic anhydrase 2013: 1856:carbonic anhydrase 1803: 1507: 1460:enzyme promiscuity 1388: 1340:A small number of 1275: 1214:chemical mechanism 1076:structural biology 880: 801: 741:Metabolic pathways 713:chemical reactions 539:Clinical chemistry 355:Chemical synthesis 78: 9752:Process chemicals 9719: 9718: 9428: 9427: 9313:Media related to 9299: 9298: 9260:978-981-4463-92-8 9249:Suzuki H (2015). 9070:10.1021/bp990013k 8884:978-0-387-71327-4 8843:10.1021/bp000128k 8801:Malts and Malting 8591:(11): 1759–1767. 8445:(5142): 652–656. 8298:"Phenylketonuria" 8276:10.1021/cr980450y 8162:(3894): 698–700. 7960:978-981-4463-92-8 7918:10.1042/bj3230001 7799:10.1242/jcs.00384 7767:978-981-4463-92-8 7669:(10): 2971–2995. 7413:(14): 7945–7958. 7329:(11): 1569–1582. 7286:10.4155/fmc.10.21 7244:10.1021/cr030102i 7033:(11): N272–N273. 6886:10.1021/bi2002289 6880:(21): 4402–4410. 6841:10.1042/bj0190338 6792:10.1021/bi201284u 6786:(39): 8264–8269. 6545:10.1021/bi0480279 6481:978-1-118-91840-1 6314:10.1021/ar400084s 6170:978-0-486-65460-7 6062:10.1021/cr0503106 6034:978-0-7167-1615-0 6023:Fersht A (1985). 5579:(5786): 518–520. 5464:Krauss G (2003). 5450:978-981-4463-92-8 5373:(15): 1248–1259. 5262:(11): 1599–1600. 5215:(4096): 223–230. 5142:978-0-470-01617-6 4988:(4986): 757–761. 4307:Molecular machine 4258: 4257: 4141:Molecular biology 3974:Make low-calorie 3816:chemical industry 3743:ultraviolet light 3673:Tay–Sachs disease 3591:that has a lower 3482:enzyme repression 3474:drug interactions 3390:glycogen synthase 3293:metabolic pathway 3241:digestive systems 3157: 3156: 2982:Lipase (stomach) 2869:citric acid cycle 2865:negative feedback 2778:allosteric effect 2373:G. E. Briggs 2279:activation energy 2275: 2274: 2231: 2218: 2213: 2210: 2200: 2188: 2170: 2155: 2154: 2111: 2098: 2093: 2090: 2080: 2068: 2050: 2017:Activation energy 2005:activation energy 2001:chemical reaction 1841:prosthetic groups 1825:organic compounds 1738: 1737: 1730: 1573:Gibbs free energy 1569:activation energy 1523:Induced fit model 1519:enzymes achieve. 1391:Substrate binding 1285:globular proteins 1279:Protein structure 1127:for enzymes, the 1123:have developed a 809:activation energy 747:and the field of 666: 665: 505:Molecular biology 448:Peptide synthesis 443:Organic synthesis 438:One-pot synthesis 373:Bioretrosynthesis 102:Chemistry of life 16:(Redirected from 9759: 9599:Hanes–Woolf plot 9542:Enzyme activator 9537:Enzyme inhibitor 9511:Enzyme catalysis 9455: 9448: 9441: 9432: 9431: 9347: 9340: 9333: 9324: 9323: 9312: 9290: 9264: 9232: 9230: 9228: 9219:. Archived from 9192: 9191: 9184: 9172: 9154: 9142: 9141: 9123: 9117: 9116: 9096: 9090: 9089: 9053: 9047: 9046: 9026: 9020: 9019: 9017: 9015: 8996: 8987: 8986: 8958: 8952: 8951: 8949: 8925: 8919: 8918: 8916: 8914: 8909:on 26 March 2015 8895: 8889: 8888: 8873:Tarté R (2008). 8870: 8864: 8863: 8845: 8821: 8815: 8814: 8796: 8785: 8784: 8756: 8747: 8746: 8710: 8701: 8700: 8690: 8650: 8644: 8643: 8615: 8609: 8608: 8580: 8574: 8573: 8545: 8539: 8538: 8510: 8504: 8503: 8485: 8479: 8478: 8459:10.1038/218652a0 8434: 8428: 8427: 8417: 8385: 8379: 8378: 8368: 8358: 8334: 8328: 8327: 8325: 8323: 8312: 8306: 8305: 8294: 8288: 8287: 8270:(8): 2137–2160. 8264:Chemical Reviews 8259: 8253: 8252: 8224: 8218: 8217: 8215: 8213: 8202: 8196: 8195: 8151: 8145: 8144: 8134: 8110: 8104: 8103: 8093: 8069: 8063: 8062: 8052: 8020: 8014: 8013: 8003: 7971: 7965: 7964: 7946: 7940: 7939: 7929: 7901: 7895: 7894: 7876: 7870: 7869: 7859: 7827: 7821: 7820: 7810: 7778: 7772: 7771: 7753: 7740: 7739: 7729: 7719: 7695: 7689: 7688: 7678: 7654: 7648: 7647: 7619: 7613: 7612: 7602: 7570: 7564: 7563: 7553: 7521: 7515: 7514: 7496: 7472: 7466: 7465: 7439: 7433: 7432: 7422: 7398: 7392: 7391: 7355: 7349: 7348: 7338: 7314: 7308: 7307: 7297: 7265: 7256: 7255: 7232:Chemical Reviews 7227: 7221: 7220: 7210: 7186: 7180: 7179: 7144:Cornish-Bowden A 7140: 7134: 7133: 7099: 7090: 7084: 7083: 7073: 7049: 7043: 7042: 7022: 7016: 7015: 6997: 6984: 6983: 6939: 6933: 6932: 6904: 6898: 6897: 6869: 6863: 6862: 6852: 6820: 6814: 6813: 6803: 6771: 6759: 6753: 6752: 6726: 6720: 6719: 6701: 6695: 6694: 6672: 6666: 6665: 6655: 6645: 6613: 6607: 6606: 6604: 6602: 6591: 6585: 6584: 6566: 6557: 6556: 6539:(4): 1097–1105. 6527: 6521: 6520: 6492: 6486: 6485: 6467: 6461: 6460: 6458: 6456: 6440: 6434: 6433: 6389: 6383: 6382: 6372: 6361:10.1039/b819720b 6340: 6334: 6333: 6297: 6291: 6290: 6272: 6240: 6234: 6233: 6223: 6213: 6181: 6175: 6174: 6156: 6150: 6149: 6105: 6099: 6098: 6080: 6074: 6073: 6056:(8): 3210–3235. 6050:Chemical Reviews 6045: 6039: 6038: 6020: 6014: 6013: 6003: 5993: 5961: 5955: 5954: 5928: 5922: 5921: 5893: 5887: 5886: 5876: 5866: 5834: 5828: 5827: 5815: 5801: 5795: 5790:From page 2992: 5789: 5765: 5759: 5758: 5748: 5724: 5718: 5717: 5689: 5683: 5682: 5654: 5648: 5647: 5619: 5613: 5612: 5568: 5562: 5561: 5525: 5519: 5518: 5490: 5484: 5483: 5461: 5455: 5454: 5436: 5427: 5426: 5424: 5422: 5407: 5401: 5400: 5382: 5358: 5352: 5351: 5341: 5317: 5311: 5310: 5288: 5282: 5281: 5271: 5247: 5241: 5240: 5204: 5198: 5197: 5187: 5177: 5153: 5147: 5146: 5120: 5114: 5113: 5111: 5109: 5089: 5083: 5082: 5080: 5078: 5063: 5057: 5056: 5028: 5022: 5021: 5002:10.1038/206757a0 4977: 4971: 4970: 4968: 4966: 4952: 4946: 4945: 4935: 4911: 4895: 4889: 4887: 4864: 4858: 4857: 4855: 4853: 4838: 4832: 4831: 4829: 4827: 4822:. Nobelprize.org 4816:"Eduard Buchner" 4812: 4806: 4805: 4783: 4777: 4767: 4754:Kühne W (1877). 4750: 4744: 4743: 4715: 4709: 4708: 4692: 4686: 4685: 4671: 4665: 4664: 4649: 4643: 4642: 4614: 4608: 4607: 4563: 4557: 4556: 4546: 4514: 4508: 4507: 4497: 4465: 4459: 4458: 4430: 4424: 4423: 4422: 4416: 4396: 4313:Enzyme databases 4291: 4286: 4285: 4277: 4272: 4271: 4049:Camembert cheese 3966:Amyloglucosidase 3924:Brewing industry 3874:Pretreatment of 3850:Biofuel industry 3834: 3833: 3821:organic solvents 3767:gene duplication 3663:Genetic disorder 3640: 3458:beta-lactam ring 3442:enzyme induction 3406:chymotrypsinogen 3206:active transport 3153:Highly alkaline 2946: 2943: 2842:to the protein. 2742:Enzyme inhibitor 2722: 2711: 2680:, respectively. 2679: 2677: 2676: 2671: 2669: 2668: 2660: 2659: 2642: 2640: 2639: 2634: 2632: 2631: 2623: 2622: 2615: 2614: 2606: 2605: 2598: 2597: 2581: 2579: 2578: 2573: 2571: 2570: 2569: 2546: 2544: 2543: 2538: 2536: 2535: 2534: 2524: 2519: 2518: 2517: 2361:Leonor Michaelis 2340:Saturation curve 2336: 2315:enzyme catalysis 2310: 2283:transition state 2269: 2251: 2249: 2248: 2243: 2241: 2239: 2236: 2229: 2226: 2223: 2216: 2214: 2211: 2208: 2202: 2198: 2196: 2193: 2186: 2181: 2178: 2175: 2168: 2157: 2149: 2131: 2129: 2128: 2123: 2121: 2119: 2116: 2109: 2106: 2103: 2096: 2094: 2091: 2088: 2082: 2078: 2076: 2073: 2066: 2061: 2058: 2055: 2048: 2037: 2009:transition state 1919:tetrahydrofolate 1800: 1733: 1726: 1722: 1719: 1713: 1690: 1682: 1641:Protein dynamics 1559:Enzyme catalysis 1540:, the substrate 1504: 1498: 1385: 1366:enzyme structure 1364:Organisation of 1331:allosteric sites 1271:rate of reaction 1172:of various bonds 1155:functional group 807:by lowering its 737:enzyme catalysis 711:by accelerating 702: 701: 698: 697: 694: 691: 688: 685: 682: 679: 658: 651: 644: 631: 626: 625: 515:Chemical biology 433:Mechanosynthesis 408:Electrosynthesis 99: 80: 79: 75: 21: 9767: 9766: 9762: 9761: 9760: 9758: 9757: 9756: 9722: 9721: 9720: 9715: 9627:Oxidoreductases 9613: 9589:Enzyme kinetics 9577: 9573:List of enzymes 9546: 9515: 9486:Catalytic triad 9464: 9459: 9429: 9424: 9356: 9351: 9305: 9300: 9287: 9261: 9237: 9226: 9224: 9217: 9186: 9181: 9151: 9149:Further reading 9146: 9145: 9138: 9124: 9120: 9097: 9093: 9054: 9050: 9027: 9023: 9013: 9011: 8998: 8997: 8990: 8959: 8955: 8926: 8922: 8912: 8910: 8897: 8896: 8892: 8885: 8871: 8867: 8822: 8818: 8811: 8797: 8788: 8757: 8750: 8711: 8704: 8651: 8647: 8616: 8612: 8581: 8577: 8546: 8542: 8521:(11): 403–405. 8511: 8507: 8500: 8486: 8482: 8435: 8431: 8386: 8382: 8335: 8331: 8321: 8319: 8314: 8313: 8309: 8296: 8295: 8291: 8260: 8256: 8225: 8221: 8211: 8209: 8204: 8203: 8199: 8152: 8148: 8125:(10): 697–702. 8111: 8107: 8070: 8066: 8021: 8017: 7972: 7968: 7961: 7947: 7943: 7902: 7898: 7891: 7877: 7873: 7828: 7824: 7779: 7775: 7768: 7754: 7743: 7696: 7692: 7655: 7651: 7620: 7616: 7571: 7567: 7522: 7518: 7473: 7469: 7454: 7440: 7436: 7399: 7395: 7356: 7352: 7315: 7311: 7266: 7259: 7228: 7224: 7187: 7183: 7141: 7137: 7097: 7091: 7087: 7050: 7046: 7023: 7019: 7012: 6998: 6987: 6940: 6936: 6915:(10): 597–604. 6905: 6901: 6870: 6866: 6821: 6817: 6760: 6756: 6741: 6727: 6723: 6716: 6706:Bioenergetics 3 6702: 6698: 6691: 6673: 6669: 6614: 6610: 6600: 6598: 6593: 6592: 6588: 6581: 6567: 6560: 6528: 6524: 6493: 6489: 6482: 6468: 6464: 6454: 6452: 6441: 6437: 6390: 6386: 6341: 6337: 6298: 6294: 6241: 6237: 6182: 6178: 6171: 6157: 6153: 6106: 6102: 6095: 6081: 6077: 6046: 6042: 6035: 6021: 6017: 5962: 5958: 5943: 5929: 5925: 5894: 5890: 5835: 5831: 5824: 5802: 5798: 5766: 5762: 5739:(4): R91–R105. 5725: 5721: 5690: 5686: 5655: 5651: 5620: 5616: 5569: 5565: 5526: 5522: 5491: 5487: 5480: 5462: 5458: 5451: 5437: 5430: 5420: 5418: 5409: 5408: 5404: 5359: 5355: 5318: 5314: 5307: 5289: 5285: 5248: 5244: 5205: 5201: 5154: 5150: 5143: 5121: 5117: 5107: 5105: 5090: 5086: 5076: 5074: 5064: 5060: 5029: 5025: 4978: 4974: 4964: 4962: 4954: 4953: 4949: 4896: 4892: 4865: 4861: 4851: 4849: 4840: 4839: 4835: 4825: 4823: 4814: 4813: 4809: 4802: 4784: 4780: 4774:zu bezeichnen." 4751: 4747: 4726:(12): 511–515. 4716: 4712: 4693: 4689: 4672: 4668: 4650: 4646: 4615: 4611: 4574:(5194): 90–93. 4564: 4560: 4515: 4511: 4466: 4462: 4431: 4427: 4417: 4413: 4397: 4352: 4347: 4315: 4302:List of enzymes 4287: 4280: 4273: 4266: 4263: 4232:Starch industry 4169:recombinant DNA 4066:Food processing 3812: 3806: 3751: 3731:cancer syndrome 3684:phenylketonuria 3665: 3632: 3617:phenylketonuria 3605: 3569:gene expression 3550: 3532:and the acidic 3520:. In addition, 3496:. For example, 3490: 3470:drug metabolism 3454:beta-lactamases 3438:gene regulation 3426: 3386:phosphorylation 3370:phosphorylation 3362: 3337: 3329: 3285: 3263:and eventually 3162: 3092:Cholinesterase 3032:Acidic-neutral 3015:Amylase (malt) 2955:pH description 2936: 2856: 2832: 2823:mixed inhibitor 2819: 2806: 2799: 2795: 2786: 2784:Non-competitive 2757: 2752: 2744: 2738: 2737: 2736: 2735: 2734: 2723: 2714: 2713: 2712: 2701: 2661: 2655: 2654: 2653: 2648: 2645: 2644: 2624: 2618: 2617: 2616: 2607: 2601: 2600: 2599: 2593: 2589: 2587: 2584: 2583: 2559: 2558: 2554: 2552: 2549: 2548: 2530: 2529: 2525: 2520: 2507: 2506: 2502: 2500: 2497: 2496: 2451: 2444: 2433:turnover number 2430: 2423: 2416: 2405: 2396: 2353: 2351:Enzyme kinetics 2347: 2346: 2345: 2344: 2343: 2337: 2328: 2327: 2326: 2321:(S) to produce 2311: 2300: 2259: 2237: 2232: 2224: 2219: 2207: 2201: 2194: 2189: 2180: 2176: 2171: 2166: 2164: 2161: 2160: 2139: 2117: 2112: 2104: 2099: 2087: 2081: 2074: 2069: 2060: 2056: 2051: 2046: 2044: 2041: 2040: 2027: 2015:Main articles: 1993: 1891: 1883:DNA polymerases 1809: 1792: 1773: 1756: 1750: 1734: 1723: 1717: 1714: 1703: 1691: 1680: 1643: 1637: 1621:catalytic triad 1565: 1555: 1529:Daniel Koshland 1525: 1512: 1500: 1490: 1393: 1377: 1358: 1281: 1263:Q10 coefficient 1255: 1168:: catalyze the 1140:Oxidoreductases 1100:. Examples are 1094:Enzyme activity 1084: 1025:James B. Sumner 968:, and the word 901:French chemist 872: 864:meat tenderizer 676: 672: 662: 621: 614: 613: 599: 591: 590: 589: 588: 498: 490: 489: 488: 487: 478:Total synthesis 356: 348: 347: 346: 345: 191: 183: 182: 168: 160: 159: 150:Gene expression 135: 127: 104: 67: 35: 28: 23: 22: 15: 12: 11: 5: 9765: 9755: 9754: 9749: 9744: 9739: 9734: 9717: 9716: 9714: 9713: 9700: 9687: 9674: 9661: 9648: 9635: 9621: 9619: 9615: 9614: 9612: 9611: 9606: 9601: 9596: 9591: 9585: 9583: 9579: 9578: 9576: 9575: 9570: 9565: 9560: 9554: 9552: 9551:Classification 9548: 9547: 9545: 9544: 9539: 9534: 9529: 9523: 9521: 9517: 9516: 9514: 9513: 9508: 9503: 9498: 9493: 9488: 9483: 9478: 9472: 9470: 9466: 9465: 9458: 9457: 9450: 9443: 9435: 9426: 9425: 9423: 9422: 9417: 9412: 9407: 9402: 9397: 9392: 9387: 9382: 9377: 9372: 9367: 9361: 9358: 9357: 9354:Food chemistry 9350: 9349: 9342: 9335: 9327: 9319: 9318: 9304: 9303:External links 9301: 9297: 9296: 9292: 9291: 9286:978-3527330744 9285: 9271: 9270: 9266: 9265: 9259: 9245: 9244: 9239: 9235: 9234: 9215: 9199: 9198: 9194: 9193: 9179: 9161: 9160: 9152: 9150: 9147: 9144: 9143: 9136: 9118: 9107:(3): 190–194. 9091: 9064:(2): 147–157. 9048: 9021: 8988: 8969:(5): 373–403. 8953: 8940:(2): 169–184. 8920: 8890: 8883: 8865: 8836:(6): 958–965. 8816: 8810:978-0412298004 8809: 8786: 8767:(4): 345–351. 8748: 8702: 8645: 8626:(4): 395–400. 8610: 8575: 8540: 8505: 8499:978-1437703146 8498: 8480: 8429: 8400:(3): 151–159. 8380: 8329: 8307: 8289: 8254: 8235:(2): 103–125. 8219: 8197: 8146: 8105: 8084:(3): 429–438. 8064: 8035:(4): 282–293. 8015: 7986:(4): 541–551. 7966: 7959: 7941: 7896: 7890:978-0748760114 7889: 7871: 7842:(2): 153–158. 7822: 7773: 7766: 7741: 7690: 7649: 7630:(2): 163–175. 7614: 7585:(1): 123–142. 7565: 7536:(4): 780–794. 7516: 7487:(2): 225–236. 7467: 7452: 7434: 7393: 7350: 7309: 7280:(6): 949–964. 7257: 7238:(2): 395–424. 7222: 7195:SLAS Discovery 7181: 7135: 7085: 7064:(4): 340–341. 7058:The Oncologist 7044: 7017: 7010: 6985: 6934: 6899: 6864: 6835:(2): 338–339. 6815: 6754: 6739: 6721: 6714: 6696: 6690:978-0781749916 6689: 6667: 6608: 6586: 6579: 6558: 6522: 6503:(9): 359–363. 6487: 6480: 6462: 6435: 6384: 6355:(3): 207–216. 6335: 6308:(1): 149–156. 6292: 6235: 6176: 6169: 6151: 6100: 6094:978-1464109621 6093: 6075: 6040: 6033: 6015: 5956: 5941: 5923: 5904:(5): 619–629. 5888: 5829: 5822: 5796: 5780:(3): 2985–93. 5760: 5719: 5684: 5649: 5614: 5563: 5542:10.1038/nrm804 5536:(5): 364–376. 5520: 5501:(4): 305–313. 5485: 5478: 5456: 5449: 5428: 5402: 5353: 5312: 5306:978-1405119221 5305: 5283: 5242: 5199: 5162:Biology Direct 5148: 5141: 5115: 5084: 5058: 5039:(7): 287–289. 5023: 4972: 4960:Nobelprize.org 4947: 4926:(4): R77–R81. 4890: 4859: 4846:Nobelprize.org 4833: 4807: 4800: 4778: 4745: 4710: 4687: 4666: 4644: 4625:(6): 465–469. 4609: 4558: 4509: 4480:(2): 323–334. 4460: 4441:(2): 537–544. 4425: 4411: 4349: 4348: 4346: 4343: 4342: 4341: 4336: 4331: 4326: 4321: 4314: 4311: 4310: 4309: 4304: 4299: 4293: 4292: 4278: 4275:Biology portal 4262: 4259: 4256: 4255: 4240: 4235: 4227: 4226: 4223:contact lenses 4219: 4214: 4206: 4205: 4194: 4188:hemicellulases 4181: 4178:Paper industry 4173: 4172: 4157: 4144: 4136: 4135: 4128: 4118: 4117: 4114:hypoallergenic 4110: 4104: 4103: 4092: 4086: 4085: 4074: 4069: 4061: 4060: 4045: 4039: 4038: 4028: 4023: 4020:Dairy industry 4015: 4014: 4008: 4003: 3995: 3994: 3987: 3980: 3979: 3972: 3962: 3961: 3954: 3952:Betaglucanases 3948: 3947: 3940: 3927: 3919: 3918: 3911: 3905: 3904: 3901: 3888: 3880: 3879: 3872: 3866: 3865: 3858: 3853: 3845: 3844: 3841: 3838: 3808:Main article: 3805: 3802: 3750: 3747: 3677:hexosaminidase 3623:substrate and 3604: 3601: 3549: 3546: 3489: 3486: 3425: 3422: 3420:or proenzyme. 3374:myristoylation 3361: 3358: 3336: 3333: 3328: 3325: 3284: 3281: 3161: 3158: 3155: 3154: 3151: 3148: 3144: 3143: 3140: 3137: 3133: 3132: 3129: 3126: 3122: 3121: 3118: 3115: 3111: 3110: 3107: 3104: 3100: 3099: 3096: 3093: 3089: 3088: 3085: 3082: 3078: 3077: 3074: 3071: 3067: 3066: 3063: 3060: 3056: 3055: 3052: 3049: 3045: 3044: 3041: 3038: 3034: 3033: 3030: 3027: 3023: 3022: 3019: 3016: 3012: 3011: 3008: 3005: 3001: 3000: 2997: 2994: 2990: 2989: 2986: 2983: 2979: 2978: 2975: 2972: 2968: 2967: 2966:Highly acidic 2964: 2961: 2957: 2956: 2953: 2950: 2935: 2932: 2890:used to treat 2855: 2852: 2831: 2828: 2818: 2815: 2805: 2802: 2797: 2793: 2785: 2782: 2756: 2753: 2751: 2748: 2740:Main article: 2724: 2717: 2716: 2715: 2706: 2705: 2704: 2703: 2702: 2700: 2697: 2667: 2664: 2658: 2652: 2630: 2627: 2621: 2613: 2610: 2604: 2596: 2592: 2568: 2565: 2562: 2557: 2533: 2528: 2523: 2516: 2513: 2510: 2505: 2454:rate constants 2449: 2442: 2428: 2421: 2414: 2403: 2394: 2349:Main article: 2338: 2331: 2330: 2329: 2312: 2305: 2304: 2303: 2302: 2301: 2299: 2296: 2273: 2272: 2263: 2261: 2260:concentration) 2257: 2235: 2222: 2205: 2192: 2184: 2174: 2153: 2152: 2143: 2141: 2140:concentration) 2137: 2115: 2102: 2085: 2072: 2064: 2054: 1992: 1991:Thermodynamics 1989: 1969: 1968: 1962: 1955: 1949: 1943: 1890: 1887: 1805:Main article: 1772: 1769: 1752:Main article: 1749: 1746: 1736: 1735: 1694: 1692: 1685: 1679: 1676: 1656:protein domain 1636: 1633: 1609: 1608: 1607: 1606: 1599: 1593: 1592: 1591: 1585: 1584: 1583: 1554: 1551: 1545:noise via the 1524: 1521: 1511: 1508: 1445:RNA polymerase 1440:DNA polymerase 1421:stereospecific 1417:regioselective 1413:chemoselective 1392: 1389: 1357: 1354: 1254: 1251: 1210: 1209: 1202: 1199:covalent bonds 1191: 1180: 1173: 1162: 1147: 1110:DNA polymerase 1083: 1080: 1010:DNA polymerase 976:Eduard Buchner 878:Eduard Buchner 871: 868: 765:, also called 664: 663: 661: 660: 653: 646: 638: 635: 634: 633: 632: 616: 615: 612: 611: 606: 600: 597: 596: 593: 592: 587: 586: 581: 576: 571: 566: 561: 556: 551: 546: 544:Neurochemistry 541: 536: 535: 534: 524: 523: 522: 512: 507: 501: 500: 499: 496: 495: 492: 491: 486: 485: 480: 475: 470: 465: 460: 458:Retrosynthesis 455: 453:Radiosynthesis 450: 445: 440: 435: 430: 425: 420: 415: 410: 405: 400: 398:Direct process 395: 390: 385: 383:Chemosynthesis 380: 375: 370: 365: 359: 358: 357: 354: 353: 350: 349: 344: 343: 338: 333: 326: 325: 324: 314: 304: 303: 302: 292: 287: 282: 272: 267: 262: 257: 252: 247: 246: 245: 235: 230: 220: 215: 210: 205: 194: 193: 192: 189: 188: 185: 184: 181: 180: 175: 169: 166: 165: 162: 161: 158: 157: 152: 147: 142: 136: 134:Key components 133: 132: 129: 128: 126: 125: 120: 115: 109: 106: 105: 100: 92: 91: 85: 84: 26: 9: 6: 4: 3: 2: 9764: 9753: 9750: 9748: 9745: 9743: 9740: 9738: 9735: 9733: 9730: 9729: 9727: 9711: 9707: 9706: 9701: 9698: 9694: 9693: 9688: 9685: 9681: 9680: 9675: 9672: 9668: 9667: 9662: 9659: 9655: 9654: 9649: 9646: 9642: 9641: 9636: 9633: 9629: 9628: 9623: 9622: 9620: 9616: 9610: 9607: 9605: 9602: 9600: 9597: 9595: 9592: 9590: 9587: 9586: 9584: 9580: 9574: 9571: 9569: 9568:Enzyme family 9566: 9564: 9561: 9559: 9556: 9555: 9553: 9549: 9543: 9540: 9538: 9535: 9533: 9532:Cooperativity 9530: 9528: 9525: 9524: 9522: 9518: 9512: 9509: 9507: 9504: 9502: 9499: 9497: 9494: 9492: 9491:Oxyanion hole 9489: 9487: 9484: 9482: 9479: 9477: 9474: 9473: 9471: 9467: 9463: 9456: 9451: 9449: 9444: 9442: 9437: 9436: 9433: 9421: 9418: 9416: 9413: 9411: 9408: 9406: 9403: 9401: 9398: 9396: 9395:Fortification 9393: 9391: 9388: 9386: 9383: 9381: 9378: 9376: 9373: 9371: 9370:Carbohydrates 9368: 9366: 9363: 9362: 9359: 9355: 9348: 9343: 9341: 9336: 9334: 9329: 9328: 9325: 9321: 9316: 9311: 9307: 9306: 9295: 9288: 9282: 9278: 9273: 9272: 9268: 9267: 9262: 9256: 9252: 9247: 9246: 9242: 9241: 9240: 9238: 9222: 9218: 9216:84-370-3328-4 9212: 9208: 9207: 9201: 9200: 9196: 9195: 9190: 9182: 9180:0-7167-3051-0 9176: 9171: 9170: 9163: 9162: 9158: 9157: 9156: 9155: 9139: 9137:9780080926551 9133: 9129: 9122: 9114: 9110: 9106: 9102: 9095: 9087: 9083: 9079: 9075: 9071: 9067: 9063: 9059: 9052: 9044: 9040: 9036: 9032: 9025: 9009: 9005: 9001: 8995: 8993: 8984: 8980: 8976: 8972: 8968: 8964: 8957: 8948: 8943: 8939: 8935: 8931: 8924: 8908: 8904: 8900: 8894: 8886: 8880: 8876: 8869: 8861: 8857: 8853: 8849: 8844: 8839: 8835: 8831: 8827: 8820: 8812: 8806: 8802: 8795: 8793: 8791: 8782: 8778: 8774: 8770: 8766: 8762: 8755: 8753: 8744: 8740: 8736: 8732: 8728: 8724: 8720: 8716: 8709: 8707: 8698: 8694: 8689: 8684: 8680: 8676: 8672: 8668: 8664: 8660: 8656: 8649: 8641: 8637: 8633: 8629: 8625: 8621: 8614: 8606: 8602: 8598: 8594: 8590: 8586: 8579: 8571: 8567: 8563: 8559: 8555: 8551: 8544: 8536: 8532: 8528: 8524: 8520: 8516: 8509: 8501: 8495: 8491: 8484: 8476: 8472: 8468: 8464: 8460: 8456: 8452: 8448: 8444: 8440: 8433: 8425: 8421: 8416: 8411: 8407: 8403: 8399: 8395: 8391: 8384: 8376: 8372: 8367: 8362: 8357: 8352: 8348: 8344: 8340: 8333: 8317: 8311: 8303: 8299: 8293: 8285: 8281: 8277: 8273: 8269: 8265: 8258: 8250: 8246: 8242: 8238: 8234: 8230: 8223: 8207: 8201: 8193: 8189: 8185: 8181: 8177: 8173: 8169: 8165: 8161: 8157: 8150: 8142: 8138: 8133: 8128: 8124: 8120: 8116: 8109: 8101: 8097: 8092: 8087: 8083: 8079: 8075: 8068: 8060: 8056: 8051: 8046: 8042: 8038: 8034: 8030: 8026: 8019: 8011: 8007: 8002: 7997: 7993: 7989: 7985: 7981: 7977: 7970: 7962: 7956: 7952: 7945: 7937: 7933: 7928: 7923: 7919: 7915: 7911: 7907: 7900: 7892: 7886: 7882: 7875: 7867: 7863: 7858: 7853: 7849: 7845: 7841: 7837: 7833: 7826: 7818: 7814: 7809: 7804: 7800: 7796: 7792: 7788: 7784: 7777: 7769: 7763: 7759: 7752: 7750: 7748: 7746: 7737: 7733: 7728: 7723: 7718: 7713: 7709: 7705: 7701: 7694: 7686: 7682: 7677: 7672: 7668: 7664: 7660: 7653: 7645: 7641: 7637: 7633: 7629: 7625: 7618: 7610: 7606: 7601: 7596: 7592: 7588: 7584: 7580: 7576: 7569: 7561: 7557: 7552: 7547: 7543: 7539: 7535: 7531: 7527: 7520: 7512: 7508: 7504: 7500: 7495: 7490: 7486: 7482: 7478: 7471: 7463: 7459: 7455: 7449: 7445: 7438: 7430: 7426: 7421: 7416: 7412: 7408: 7404: 7397: 7389: 7385: 7381: 7377: 7373: 7369: 7365: 7361: 7354: 7346: 7342: 7337: 7332: 7328: 7324: 7320: 7313: 7305: 7301: 7296: 7291: 7287: 7283: 7279: 7275: 7271: 7264: 7262: 7253: 7249: 7245: 7241: 7237: 7233: 7226: 7218: 7214: 7209: 7204: 7200: 7196: 7192: 7185: 7177: 7173: 7169: 7165: 7161: 7157: 7153: 7149: 7145: 7139: 7131: 7127: 7123: 7119: 7115: 7111: 7107: 7103: 7096: 7089: 7081: 7077: 7072: 7067: 7063: 7059: 7055: 7048: 7040: 7036: 7032: 7028: 7021: 7013: 7011:1-85578-158-1 7007: 7003: 6996: 6994: 6992: 6990: 6981: 6977: 6973: 6969: 6965: 6961: 6957: 6953: 6949: 6945: 6938: 6930: 6926: 6922: 6918: 6914: 6910: 6903: 6895: 6891: 6887: 6883: 6879: 6875: 6868: 6860: 6856: 6851: 6846: 6842: 6838: 6834: 6830: 6826: 6819: 6811: 6807: 6802: 6797: 6793: 6789: 6785: 6781: 6777: 6769: 6766:(in German). 6765: 6758: 6750: 6746: 6742: 6740:9783527806461 6736: 6732: 6725: 6717: 6715:0-12-518121-3 6711: 6707: 6700: 6692: 6686: 6682: 6678: 6671: 6663: 6659: 6654: 6649: 6644: 6639: 6635: 6631: 6627: 6623: 6619: 6612: 6596: 6590: 6582: 6580:0-88275-258-8 6576: 6572: 6565: 6563: 6554: 6550: 6546: 6542: 6538: 6534: 6526: 6518: 6514: 6510: 6506: 6502: 6498: 6491: 6483: 6477: 6473: 6466: 6450: 6446: 6439: 6431: 6427: 6423: 6419: 6415: 6411: 6407: 6403: 6399: 6395: 6388: 6380: 6376: 6371: 6366: 6362: 6358: 6354: 6350: 6346: 6339: 6331: 6327: 6323: 6319: 6315: 6311: 6307: 6303: 6296: 6288: 6284: 6280: 6276: 6271: 6266: 6262: 6258: 6254: 6250: 6246: 6239: 6231: 6227: 6222: 6217: 6212: 6207: 6203: 6199: 6195: 6191: 6187: 6180: 6172: 6166: 6162: 6155: 6147: 6143: 6139: 6135: 6131: 6127: 6123: 6119: 6115: 6111: 6104: 6096: 6090: 6086: 6079: 6071: 6067: 6063: 6059: 6055: 6051: 6044: 6036: 6030: 6026: 6019: 6011: 6007: 6002: 5997: 5992: 5987: 5983: 5979: 5975: 5971: 5967: 5960: 5952: 5948: 5944: 5942:0-470-00379-0 5938: 5934: 5927: 5919: 5915: 5911: 5907: 5903: 5899: 5892: 5884: 5880: 5875: 5870: 5865: 5860: 5856: 5852: 5849:(2): 98–104. 5848: 5844: 5840: 5833: 5825: 5823:0-87893-106-6 5819: 5814: 5813: 5807: 5800: 5793: 5787: 5783: 5779: 5776:(in German). 5775: 5771: 5764: 5756: 5752: 5747: 5742: 5738: 5734: 5730: 5723: 5715: 5711: 5707: 5703: 5699: 5695: 5688: 5680: 5676: 5672: 5668: 5664: 5660: 5653: 5645: 5641: 5637: 5633: 5629: 5625: 5618: 5610: 5606: 5602: 5598: 5594: 5590: 5586: 5582: 5578: 5574: 5567: 5559: 5555: 5551: 5547: 5543: 5539: 5535: 5531: 5524: 5516: 5512: 5508: 5504: 5500: 5496: 5489: 5481: 5479:9783527605767 5475: 5471: 5467: 5460: 5452: 5446: 5442: 5435: 5433: 5416: 5412: 5406: 5398: 5394: 5390: 5386: 5381: 5376: 5372: 5368: 5367:FASEB Journal 5364: 5357: 5349: 5345: 5340: 5335: 5331: 5327: 5323: 5316: 5308: 5302: 5298: 5294: 5287: 5279: 5275: 5270: 5265: 5261: 5257: 5253: 5246: 5238: 5234: 5230: 5226: 5222: 5218: 5214: 5210: 5203: 5195: 5191: 5186: 5181: 5176: 5171: 5167: 5163: 5159: 5152: 5144: 5138: 5134: 5130: 5126: 5119: 5103: 5099: 5095: 5088: 5073: 5069: 5062: 5054: 5050: 5046: 5042: 5038: 5034: 5027: 5019: 5015: 5011: 5007: 5003: 4999: 4995: 4991: 4987: 4983: 4976: 4961: 4957: 4951: 4943: 4939: 4934: 4929: 4925: 4921: 4917: 4909: 4905: 4902:: 1359–1381. 4901: 4894: 4885: 4881: 4880: 4873: 4869: 4868:Émile Duclaux 4863: 4847: 4843: 4837: 4821: 4817: 4811: 4803: 4801:9780199743766 4797: 4793: 4789: 4782: 4775: 4771: 4766:(3): 190–193. 4765: 4761: 4757: 4749: 4741: 4737: 4733: 4729: 4725: 4721: 4714: 4706: 4702: 4698: 4691: 4683: 4682: 4678: 4670: 4662: 4658: 4654: 4653:de Réaumur RA 4648: 4640: 4636: 4632: 4628: 4624: 4620: 4613: 4605: 4601: 4597: 4593: 4589: 4585: 4581: 4577: 4573: 4569: 4562: 4554: 4550: 4545: 4540: 4536: 4532: 4528: 4524: 4520: 4513: 4505: 4501: 4496: 4491: 4487: 4483: 4479: 4475: 4471: 4464: 4456: 4452: 4448: 4444: 4440: 4436: 4429: 4421: 4414: 4412:0-7167-4955-6 4408: 4404: 4403: 4395: 4393: 4391: 4389: 4387: 4385: 4383: 4381: 4379: 4377: 4375: 4373: 4371: 4369: 4367: 4365: 4363: 4361: 4359: 4357: 4355: 4350: 4340: 4337: 4335: 4332: 4330: 4327: 4325: 4322: 4320: 4317: 4316: 4308: 4305: 4303: 4300: 4298: 4295: 4294: 4290: 4284: 4279: 4276: 4270: 4265: 4253: 4249: 4245: 4241: 4239: 4236: 4234: 4233: 4224: 4220: 4218: 4215: 4213: 4212: 4211:Personal care 4208: 4203: 4199: 4195: 4193: 4189: 4185: 4182: 4180: 4179: 4175: 4170: 4166: 4162: 4158: 4156: 4152: 4148: 4145: 4143: 4142: 4138: 4133: 4129: 4127: 4123: 4120: 4115: 4111: 4109: 4106: 4101: 4097: 4093: 4091: 4088: 4083: 4079: 4075: 4073: 4070: 4068: 4067: 4058: 4054: 4050: 4046: 4044: 4041: 4036: 4032: 4029: 4027: 4024: 4022: 4021: 4012: 4009: 4007: 4004: 4002: 4001: 4000:Culinary uses 3997: 3992: 3988: 3985: 3982: 3977: 3973: 3971: 3967: 3964: 3959: 3955: 3953: 3950: 3945: 3941: 3939: 3935: 3931: 3928: 3926: 3925: 3916: 3912: 3910: 3907: 3902: 3900: 3896: 3892: 3889: 3887: 3886: 3877: 3873: 3871: 3868: 3863: 3859: 3857: 3854: 3852: 3851: 3842: 3840:Enzymes used 3839: 3836: 3835: 3832: 3830: 3826: 3822: 3817: 3811: 3801: 3798: 3796: 3792: 3788: 3784: 3780: 3776: 3772: 3768: 3764: 3760: 3756: 3746: 3744: 3740: 3736: 3732: 3728: 3724: 3720: 3716: 3711: 3709: 3705: 3701: 3697: 3693: 3692:phenylalanine 3689: 3685: 3680: 3678: 3674: 3670: 3664: 3656: 3652: 3647: 3639: 3635: 3630: 3626: 3622: 3621:Phenylalanine 3618: 3614: 3609: 3600: 3598: 3594: 3590: 3586: 3582: 3578: 3574: 3570: 3566: 3562: 3558: 3555: 3554:multicellular 3545: 3543: 3539: 3535: 3531: 3527: 3523: 3519: 3515: 3514:mitochondrion 3511: 3507: 3503: 3499: 3495: 3485: 3483: 3479: 3475: 3471: 3467: 3463: 3459: 3455: 3451: 3447: 3443: 3439: 3435: 3431: 3430:transcription 3421: 3419: 3415: 3411: 3407: 3403: 3399: 3395: 3391: 3387: 3383: 3379: 3378:glycosylation 3375: 3371: 3367: 3357: 3355: 3351: 3346: 3342: 3332: 3324: 3322: 3316: 3314: 3306: 3302: 3298: 3294: 3289: 3280: 3278: 3274: 3271:, which have 3270: 3266: 3262: 3258: 3254: 3250: 3246: 3242: 3237: 3235: 3234:neuraminidase 3231: 3227: 3223: 3222:HIV integrase 3219: 3215: 3211: 3207: 3203: 3199: 3195: 3191: 3187: 3183: 3179: 3175: 3171: 3167: 3152: 3149: 3146: 3145: 3141: 3138: 3135: 3134: 3130: 3127: 3124: 3123: 3119: 3116: 3113: 3112: 3108: 3105: 3103:Ribonuclease 3102: 3101: 3097: 3094: 3091: 3090: 3086: 3083: 3080: 3079: 3075: 3072: 3069: 3068: 3064: 3061: 3058: 3057: 3053: 3050: 3047: 3046: 3042: 3039: 3036: 3035: 3031: 3028: 3025: 3024: 3020: 3017: 3014: 3013: 3009: 3006: 3003: 3002: 2998: 2995: 2992: 2991: 2987: 2984: 2981: 2980: 2976: 2973: 2970: 2969: 2965: 2962: 2959: 2958: 2954: 2951: 2948: 2947: 2942: 2939: 2931: 2929: 2925: 2921: 2917: 2916:prostaglandin 2913: 2909: 2905: 2901: 2897: 2893: 2889: 2885: 2881: 2877: 2872: 2870: 2866: 2861: 2851: 2849: 2845: 2841: 2840:covalent bond 2837: 2827: 2824: 2814: 2811: 2804:Uncompetitive 2801: 2791: 2781: 2779: 2776:and exert an 2774: 2773:dihydrofolate 2770: 2766: 2762: 2747: 2743: 2732: 2728: 2725:The coenzyme 2721: 2710: 2696: 2694: 2690: 2686: 2681: 2665: 2662: 2650: 2628: 2625: 2611: 2608: 2594: 2590: 2555: 2526: 2521: 2503: 2494: 2490: 2486: 2482: 2478: 2474: 2470: 2466: 2462: 2461: 2455: 2448: 2441: 2436: 2434: 2427: 2420: 2413: 2409: 2402: 2398: 2393: 2389: 2388:concentration 2385: 2380: 2378: 2374: 2370: 2366: 2362: 2358: 2357:enzyme assays 2352: 2341: 2335: 2324: 2320: 2316: 2309: 2295: 2293: 2287: 2284: 2280: 2271: 2264: 2262: 2255: 2233: 2220: 2203: 2190: 2182: 2172: 2159: 2158: 2151: 2144: 2142: 2135: 2113: 2100: 2083: 2070: 2062: 2052: 2039: 2038: 2035: 2033: 2026: 2022: 2018: 2010: 2006: 2002: 1997: 1988: 1986: 1982: 1978: 1973: 1967: 1963: 1960: 1956: 1954: 1950: 1948: 1944: 1942: 1938: 1934: 1933: 1932: 1930: 1929: 1924: 1920: 1916: 1912: 1908: 1904: 1900: 1896: 1886: 1884: 1880: 1876: 1872: 1868: 1863: 1861: 1857: 1852: 1850: 1846: 1842: 1838: 1834: 1830: 1826: 1822: 1818: 1815:(e.g., metal 1814: 1808: 1799: 1795: 1790: 1786: 1785:transketolase 1782: 1777: 1768: 1766: 1762: 1755: 1745: 1742: 1732: 1729: 1721: 1711: 1707: 1701: 1700: 1695:This section 1693: 1689: 1684: 1683: 1675: 1673: 1669: 1665: 1661: 1657: 1653: 1649: 1642: 1632: 1630: 1626: 1625:oxyanion hole 1622: 1618: 1614: 1604: 1600: 1597: 1596: 1594: 1589: 1588: 1586: 1581: 1580: 1578: 1577: 1576: 1574: 1570: 1564: 1560: 1550: 1548: 1543: 1539: 1535: 1530: 1520: 1517: 1503: 1497: 1493: 1488: 1484: 1480: 1476: 1471: 1467: 1465: 1461: 1456: 1454: 1450: 1446: 1441: 1437: 1436:proof-reading 1433: 1429: 1424: 1422: 1418: 1414: 1410: 1406: 1402: 1398: 1384: 1380: 1375: 1374:peptidoglycan 1371: 1367: 1362: 1353: 1351: 1347: 1343: 1338: 1336: 1332: 1328: 1323: 1321: 1317: 1316:binding sites 1313: 1309: 1305: 1300: 1298: 1294: 1290: 1286: 1280: 1272: 1268: 1264: 1259: 1250: 1248: 1244: 1240: 1236: 1234: 1229: 1225: 1221: 1219: 1215: 1207: 1203: 1200: 1196: 1192: 1189: 1188:isomerization 1185: 1181: 1178: 1174: 1171: 1167: 1163: 1160: 1156: 1153:: transfer a 1152: 1148: 1145: 1141: 1137: 1136: 1135: 1132: 1130: 1126: 1122: 1117: 1115: 1111: 1107: 1103: 1099: 1095: 1091: 1089: 1079: 1077: 1073: 1069: 1065: 1061: 1056: 1054: 1050: 1046: 1042: 1038: 1034: 1030: 1026: 1022: 1018: 1013: 1011: 1007: 1003: 999: 995: 994: 989: 985: 981: 977: 973: 971: 967: 963: 959: 955: 952: 949: 946: 945:Ancient Greek 942: 941: 936: 935:Wilhelm Kühne 931: 928: 924: 923:Louis Pasteur 920: 916: 912: 908: 904: 903:Anselme Payen 899: 897: 893: 889: 885: 876: 867: 865: 861: 857: 853: 848: 846: 842: 838: 834: 830: 826: 822: 818: 814: 810: 806: 805:reaction rate 797: 793: 791: 787: 782: 780: 776: 772: 768: 764: 759: 756: 754: 750: 746: 742: 738: 734: 730: 727:. Almost all 726: 722: 718: 714: 710: 706: 700: 670: 659: 654: 652: 647: 645: 640: 639: 637: 636: 630: 620: 619: 618: 617: 610: 607: 605: 602: 601: 595: 594: 585: 582: 580: 577: 575: 572: 570: 567: 565: 562: 560: 557: 555: 552: 550: 547: 545: 542: 540: 537: 533: 530: 529: 528: 525: 521: 518: 517: 516: 513: 511: 508: 506: 503: 502: 494: 493: 484: 481: 479: 476: 474: 471: 469: 466: 464: 463:Semisynthesis 461: 459: 456: 454: 451: 449: 446: 444: 441: 439: 436: 434: 431: 429: 426: 424: 421: 419: 416: 414: 411: 409: 406: 404: 401: 399: 396: 394: 391: 389: 386: 384: 381: 379: 376: 374: 371: 369: 366: 364: 361: 360: 352: 351: 342: 339: 337: 336:Tetrapyrroles 334: 332: 331: 327: 323: 320: 319: 318: 315: 313: 312: 310: 305: 301: 298: 297: 296: 293: 291: 288: 286: 283: 281: 280: 278: 277:Nucleic acids 273: 271: 268: 266: 263: 261: 260:Sphingolipids 258: 256: 255:Phospholipids 253: 251: 248: 244: 241: 240: 239: 236: 234: 231: 229: 228: 226: 221: 219: 216: 214: 213:Glycoproteins 211: 209: 206: 204: 203: 201: 200:Carbohydrates 196: 195: 187: 186: 179: 176: 174: 171: 170: 164: 163: 156: 153: 151: 148: 146: 143: 141: 138: 137: 131: 130: 124: 121: 119: 116: 114: 111: 110: 108: 107: 103: 98: 94: 93: 90: 87: 86: 82: 81: 74: 70: 65: 62: 58: 54: 50: 46: 41: 37: 33: 19: 9737:Biomolecules 9705:Translocases 9702: 9689: 9676: 9663: 9650: 9640:Transferases 9637: 9624: 9481:Binding site 9461: 9379: 9320: 9293: 9276: 9250: 9236: 9225:. Retrieved 9221:the original 9205: 9169:Biochemistry 9168: 9127: 9121: 9104: 9100: 9094: 9061: 9057: 9051: 9037:(1): 21–28. 9034: 9030: 9024: 9012:. Retrieved 9008:the original 9003: 8966: 8962: 8956: 8937: 8933: 8923: 8911:. Retrieved 8907:the original 8902: 8893: 8874: 8868: 8833: 8829: 8819: 8800: 8764: 8760: 8718: 8714: 8662: 8658: 8648: 8623: 8619: 8613: 8588: 8584: 8578: 8553: 8549: 8543: 8518: 8514: 8508: 8489: 8483: 8442: 8438: 8432: 8397: 8393: 8383: 8346: 8342: 8332: 8320:. Retrieved 8310: 8301: 8292: 8267: 8263: 8257: 8232: 8228: 8222: 8210:. 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Retrieved 4819: 4810: 4791: 4781: 4773: 4769: 4763: 4759: 4748: 4723: 4719: 4713: 4704: 4700: 4690: 4680: 4676: 4669: 4660: 4656: 4647: 4622: 4618: 4612: 4571: 4567: 4561: 4526: 4522: 4512: 4477: 4473: 4463: 4438: 4434: 4428: 4402:Biochemistry 4401: 4250:and various 4230: 4209: 4176: 4139: 4132:fruit juices 4116:baby foods. 4112:Manufacture 4064: 4053:blue cheeses 4018: 3998: 3970:pullulanases 3956:Improve the 3922: 3883: 3848: 3837:Application 3828: 3813: 3799: 3752: 3739:skin cancers 3712: 3681: 3666: 3551: 3540:or reducing 3491: 3427: 3402:Chymotrypsin 3364:Examples of 3363: 3338: 3330: 3317: 3310: 3238: 3204:involved in 3194:cytoskeleton 3184:hydrolyzing 3178:phosphatases 3163: 2940: 2937: 2912:inflammation 2876:methotrexate 2873: 2857: 2833: 2830:Irreversible 2820: 2807: 2787: 2765:methotrexate 2758: 2745: 2731:methotrexate 2682: 2464: 2458: 2446: 2439: 2437: 2432: 2425: 2418: 2411: 2400: 2399: 2391: 2381: 2354: 2288: 2276: 2265: 2145: 2028: 1980: 1974: 1970: 1926: 1892: 1878: 1874: 1870: 1866: 1864: 1853: 1810: 1757: 1739: 1724: 1718:October 2023 1715: 1704:Please help 1699:verification 1696: 1648:protein loop 1644: 1610: 1566: 1538:glycosidases 1526: 1516:Emil Fischer 1513: 1457: 1425: 1394: 1339: 1324: 1301: 1282: 1267:denaturation 1242: 1238: 1237: 1227: 1223: 1222: 1211: 1206:Translocases 1158: 1151:Transferases 1133: 1125:nomenclature 1118: 1097: 1093: 1092: 1085: 1057: 1053:chymotrypsin 1020: 1014: 991: 974: 969: 961: 953: 948: 938: 932: 913:of sugar to 911:fermentation 900: 881: 849: 802: 784:An enzyme's 783: 778: 774: 770: 760: 757: 744: 668: 667: 574:parasitology 569:Bacteriology 532:Pharmacology 510:Cell biology 378:Biosynthesis 329: 328: 307: 306: 275: 274: 223: 222: 198: 197: 144: 140:Biomolecules 101: 89:Biochemistry 66:in yellow. ( 36: 32:Biocatalysis 9476:Active site 9014:28 February 9004:GMO Compass 8903:GMO Compass 8721:(1): 1–11. 8556:: 133–140. 8322:5 September 7366:: 249–284. 7201:(1): 3–20. 6764:Biochem. Z. 6601:23 February 5976:(5): e468. 5700:: 471–505. 5665:: 415–435. 5630:: 617–650. 4965:23 February 4852:23 February 4826:23 February 4663:: 266, 461. 4289:Food portal 4155:polymerases 3993:formation. 3669:homeostasis 3597:blood sugar 3585:glucokinase 3526:protonation 3522:trafficking 3518:β-oxidation 3498:fatty acids 3478:degradation 3434:translation 3398:blood sugar 3273:herbivorous 3037:Cellobiase 2952:Optimum pH 2926:and blocks 2884:cholesterol 2755:Competitive 2489:β-lactamase 2007:to reach a 1941:NAD or NADP 1917:(TPP), and 1871:apoproteins 1862:reactions. 1664:equilibrium 1650:or unit of 1627:, complete 1549:mechanism. 1534:side-chains 1409:hydrophobic 1405:hydrophilic 1401:Specificity 1320:active site 1297:hot springs 1186:: catalyze 1142:: catalyze 927:vital force 852:antibiotics 837:temperature 817:equilibrium 786:specificity 317:Amino acids 295:Nucleotides 290:Nucleosides 285:Nucleobases 265:Cholesterol 238:Fatty acids 233:Eicosanoids 57:Active site 45:glucosidase 43:The enzyme 9747:Metabolism 9726:Categories 9679:Isomerases 9653:Hydrolases 9520:Regulation 7453:8121903432 7154:(1): 3–6. 6770:: 333–369. 6455:30 October 4912:quoted in 4345:References 4202:kraft pulp 4167:to create 4151:DNA ligase 4126:pectinases 4122:Cellulases 3934:glucanases 3909:Mannanases 3870:Ligninases 3856:Cellulases 3779:methionine 3775:creatinase 3763:adaptation 3759:metabolism 3719:DNA repair 3661:See also: 3581:glycolysis 3577:hexokinase 3557:eukaryotes 3516:, through 3450:penicillin 3440:is called 3335:Regulation 3297:glycolysis 3283:Metabolism 3210:luciferase 2971:Invertase 2914:messenger 2892:retroviral 2844:Penicillin 2727:folic acid 2699:Inhibition 2582:are about 2359:. In 1913 1959:folic acid 1953:coenzyme A 1879:holoenzyme 1875:holoenzyme 1867:apoenzymes 1639:See also: 1629:hydrolysis 1557:See also: 1475:Hexokinase 1428:expression 1397:substrates 1277:See also: 1218:hexokinase 1184:Isomerases 1170:hydrolysis 1166:Hydrolases 1068:egg whites 825:activators 821:inhibitors 753:amino acid 745:enzymology 721:substrates 598:Glossaries 584:immunology 250:Glycerides 218:Glycosides 173:Biochemist 155:Metabolism 9742:Catalysis 9558:EC number 9365:Additives 8349:: 55–73. 8078:Structure 7462:818809626 7108:: 59–68. 6749:992976641 5256:Structure 5168:(1): 31. 5077:28 August 5066:Moss GP. 4920:Structure 4788:"Enzymes" 4217:Proteases 4184:Xylanases 4147:Nucleases 4102:-making. 4090:Proteases 4057:Roquefort 4031:Hydrolyze 4011:Tenderize 3938:proteases 3891:Proteases 3787:sarcosine 3755:mutations 3749:Evolution 3655:recessive 3651:autosomal 3542:cytoplasm 3538:periplasm 3530:cytoplasm 3348:called a 3345:inhibited 3341:activated 3277:cellulase 3269:ruminants 3249:proteases 3230:influenza 3214:fireflies 3202:ion pumps 3166:functions 3147:Arginase 3142:Alkaline 3131:Alkaline 3120:Alkaline 3114:Fumarase 3070:Catalase 3010:Alkaline 2689:diffusion 2663:− 2626:− 2609:− 2319:substrate 2136:; high CO 1889:Coenzymes 1837:coenzymes 1813:inorganic 1771:Cofactors 1613:proteases 1553:Catalysis 1527:In 1958, 1499:, 1464:neutrally 1453:ribosomes 1356:Mechanism 1346:ribozymes 1327:cofactors 1289:complexes 1253:Structure 1144:oxidation 998:substrate 954:(énzymon) 845:denatured 767:ribozymes 717:molecules 709:catalysts 51:into two 9582:Kinetics 9506:Cofactor 9469:Activity 9415:Vitamins 9410:Proteins 9375:Coloring 9086:26080240 9078:10194388 8860:25674881 8852:11101321 8781:12323357 8743:12058826 8697:18323453 8640:12943848 8605:16433409 8570:29316484 8424:24917953 8375:21753892 8284:11849022 8249:10527663 8100:15016359 8059:27098510 8010:20713603 7817:12615961 7736:18952571 7644:12370077 7560:11294886 7511:13999125 7388:10205781 7304:20640225 7252:15700950 7217:27703080 7176:45356060 7122:26478442 7080:10476546 6980:23465446 6972:17820893 6929:11590012 6894:21506553 6859:16743508 6810:21888353 6662:19073922 6553:15667203 6517:10470036 6430:10621930 6422:15933191 6379:19225609 6330:23988159 6279:16003488 6270:11139141 6230:11050223 6138:12947189 6070:16895325 6010:17520027 5970:PLOS ONE 5951:51720783 5918:12413546 5883:16590179 5755:10099128 5714:20235827 5679:11395413 5644:10966471 5609:40772789 5601:16873663 5558:31605786 5550:11988770 5515:15358000 5397:22853095 5278:19000810 5194:20433725 5053:10390620 4942:10801479 4872:diastase 4707:: 73–92. 4639:17889251 4553:23203881 4504:24107129 4455:28408493 4261:See also 4242:Convert 4238:Amylases 4163:and the 4130:Clarify 4098:, as in 4072:Amylases 4055:such as 4047:Produce 3991:diacetyl 3915:guar gum 3895:amylases 3829:in vitro 3783:creatine 3641:) 3593:affinity 3589:pancreas 3573:isozymes 3534:lysosome 3448:such as 3424:Quantity 3410:pancreas 3394:glycogen 3368:include 3305:pyruvate 3257:proteins 3245:amylases 3196:. Other 3128:7.8–8.7 3125:Trypsin 3109:Neutral 3106:7.0–7.5 3098:Neutral 3087:Neutral 3076:Neutral 3059:Sucrase 3051:6.1–6.8 3048:Maltase 3029:6.7–7.0 3018:4.6–5.2 2985:4.0–5.0 2963:1.5–1.6 2860:feedback 2485:fumarase 2481:catalase 2384:solution 2298:Kinetics 2256:; low CO 2204:← 2084:→ 1923:vitamins 1801:) 1761:feedback 1635:Dynamics 1615:such as 1542:molecule 1505:) 1386:) 1370:lysozyme 1350:ribosome 1293:denature 1114:isozymes 1064:lysozyme 1047:(1930), 1033:catalase 958:leavened 907:diastase 725:products 705:proteins 629:Category 579:virology 309:Proteins 270:Steroids 208:Alcohols 76:) 64:cofactor 55:sugars. 9732:Enzymes 9692:Ligases 9462:Enzymes 9390:Flavors 9380:Enzymes 9315:Enzymes 9227:27 June 9159:General 9113:2186082 8983:8573280 8913:1 March 8723:Bibcode 8688:3431203 8667:Bibcode 8659:Science 8535:8291080 8475:4171859 8467:5655953 8447:Bibcode 8415:4040760 8366:3132852 8212:1 March 8192:8473726 8184:5793973 8164:Bibcode 8156:Science 8141:8433729 8050:4915340 8001:2928026 7936:9173866 7927:1218279 7866:8452343 7808:3006448 7727:2674713 7685:2178174 7609:2030669 7503:7834742 7429:2159465 7380:9646869 7345:1464741 7295:2904065 7168:3720956 7130:1550698 6952:Bibcode 6944:Science 6850:1259181 6801:3381512 6653:2604989 6630:Bibcode 6402:Bibcode 6394:Science 6370:2898650 6322:1565147 6287:3343824 6198:Bibcode 6146:7899320 6118:Bibcode 6110:Science 6001:1868595 5978:Bibcode 5851:Bibcode 5581:Bibcode 5573:Science 5421:4 April 5389:8001737 5348:1339435 5237:4124164 5217:Bibcode 5209:Science 5185:2876114 5108:6 March 5018:4161467 5010:5891407 4990:Bibcode 4740:8595136 4604:8145198 4596:7809611 4576:Bibcode 4568:Science 4544:3531171 4495:5679212 4339:MetaCyc 4248:glucose 4196:Remove 4108:Trypsin 4100:biscuit 4043:Lipases 3986:(ALDC) 3930:Amylase 3899:lipases 3876:biomass 3795:kinases 3723:genomes 3565:tissues 3502:cytosol 3464:called 3418:zymogen 3414:stomach 3408:in the 3382:insulin 3301:glucose 3265:glucose 3261:maltose 3218:Viruses 3198:ATPases 3174:kinases 3081:Urease 3065:Acidic 3054:Acidic 3043:Acidic 3021:Acidic 2999:Acidic 2988:Acidic 2977:Acidic 2960:Pepsin 2949:Enzyme 2920:cyanide 2900:aspirin 2880:statins 2848:aspirin 2323:product 2134:tissues 1937:hydride 1928:de novo 1913:(FAD), 1909:(FMN), 1827:(e.g., 1617:trypsin 1603:entropy 1430:of the 1304:monomer 1195:Ligases 1102:lactase 1049:trypsin 1006:lactose 1002:lactase 1000:(e.g., 970:ferment 956: ' 951:ἔνζυμον 915:alcohol 833:poisons 731:in the 669:Enzymes 145:Enzymes 123:History 118:Outline 53:glucose 49:maltose 9666:Lyases 9400:Lipids 9294: 9283: 9257: 9213: 9177: 9134: 9111: 9084: 9076: 8981: 8881: 8858: 8850: 8807: 8779: 8741: 8695: 8685: 8638: 8603: 8568: 8533: 8496: 8473: 8465: 8439:Nature 8422: 8412: 8373: 8363: 8282: 8247: 8190: 8182: 8139: 8098: 8057: 8047: 8008: 7998: 7957: 7934: 7924: 7887: 7864: 7857:187630 7854: 7815: 7805: 7764: 7734: 7724: 7683: 7642: 7607: 7600:372803 7597: 7558: 7548: 7509: 7501: 7460: 7450: 7427: 7386: 7378: 7343: 7302: 7292: 7250: 7215: 7174: 7166: 7128: 7120: 7078: 7008: 6978: 6970: 6927: 6892: 6857: 6847: 6808: 6798: 6747: 6737: 6712: 6687: 6660: 6650: 6577: 6551: 6515: 6478: 6428: 6420: 6377: 6367: 6328: 6320: 6285: 6277: 6267: 6228: 6218: 6167: 6144: 6136: 6091: 6068: 6031: 6008: 5998: 5949: 5939: 5916: 5881: 5874:335371 5871: 5820: 5753: 5712: 5677: 5642: 5607: 5599: 5556: 5548: 5513: 5476: 5447: 5395: 5387: 5346: 5303: 5276: 5235: 5192: 5182: 5139: 5051: 5016: 5008: 4982:Nature 4940: 4848:. 1907 4798: 4772:Enzyme 4738: 4637: 4602: 4594: 4551: 4541: 4502: 4492: 4453: 4409: 4329:IntEnz 4324:ExPASy 4319:BRENDA 4252:syrups 4244:starch 4198:lignin 4078:starch 4035:cheese 4026:Rennin 4006:Papain 3561:organs 3384:, the 3253:starch 3232:virus 3182:myosin 2886:, and 2491:, and 2023:, and 1845:biotin 1829:flavin 1483:xylose 1432:genome 1204:EC 7, 1193:EC 6, 1182:EC 5, 1177:Lyases 1175:EC 4, 1164:EC 3, 1149:EC 2, 1138:EC 1, 1045:pepsin 1029:urease 1021:per se 984:zymase 966:pepsin 962:enzyme 940:enzyme 896:saliva 892:sugars 888:starch 779:enzyme 715:. The 703:) are 627: 330:Other: 225:Lipids 9618:Types 9420:Water 9082:S2CID 8856:S2CID 8471:S2CID 8188:S2CID 7551:32266 7507:S2CID 7384:S2CID 7172:S2CID 7126:S2CID 7098:(PDF) 6976:S2CID 6426:S2CID 6283:S2CID 6221:17266 6142:S2CID 5605:S2CID 5554:S2CID 5393:S2CID 5014:S2CID 4882:[ 4600:S2CID 4246:into 4200:from 4096:flour 3843:Uses 3510:Golgi 3462:liver 3150:10.0 2908:COX-2 2904:COX-1 2817:Mixed 2254:lungs 1899:NADPH 1860:redox 1823:) or 1571:(ΔG, 1532:acid 947: 919:yeast 829:drugs 735:need 428:LASiS 113:Index 9710:list 9703:EC7 9697:list 9690:EC6 9684:list 9677:EC5 9671:list 9664:EC4 9658:list 9651:EC3 9645:list 9638:EC2 9632:list 9625:EC1 9281:ISBN 9255:ISBN 9229:2006 9211:ISBN 9175:ISBN 9132:ISBN 9109:PMID 9074:PMID 9016:2015 8979:PMID 8915:2015 8879:ISBN 8848:PMID 8805:ISBN 8777:PMID 8739:PMID 8693:PMID 8636:PMID 8601:PMID 8566:PMID 8531:PMID 8494:ISBN 8463:PMID 8420:PMID 8371:PMID 8324:2013 8280:PMID 8245:PMID 8214:2015 8180:PMID 8137:PMID 8096:PMID 8055:PMID 8006:PMID 7955:ISBN 7932:PMID 7885:ISBN 7862:PMID 7813:PMID 7762:ISBN 7732:PMID 7681:PMID 7640:PMID 7605:PMID 7556:PMID 7499:PMID 7481:Cell 7458:OCLC 7448:ISBN 7425:PMID 7376:PMID 7341:PMID 7300:PMID 7248:PMID 7213:PMID 7164:PMID 7118:PMID 7076:PMID 7006:ISBN 6968:PMID 6925:PMID 6890:PMID 6855:PMID 6806:PMID 6745:OCLC 6735:ISBN 6710:ISBN 6685:ISBN 6658:PMID 6603:2015 6575:ISBN 6549:PMID 6513:PMID 6476:ISBN 6457:2007 6418:PMID 6375:PMID 6326:PMID 6318:OSTI 6275:PMID 6226:PMID 6165:ISBN 6134:PMID 6089:ISBN 6066:PMID 6029:ISBN 6006:PMID 5947:OCLC 5937:ISBN 5914:PMID 5879:PMID 5818:ISBN 5751:PMID 5710:PMID 5675:PMID 5640:PMID 5597:PMID 5546:PMID 5511:PMID 5474:ISBN 5445:ISBN 5423:2007 5385:PMID 5344:PMID 5301:ISBN 5274:PMID 5233:PMID 5190:PMID 5137:ISBN 5110:2015 5079:2021 5049:PMID 5006:PMID 4967:2015 4938:PMID 4854:2015 4828:2015 4796:ISBN 4736:PMID 4661:1752 4635:PMID 4592:PMID 4549:PMID 4500:PMID 4451:PMID 4407:ISBN 4334:KEGG 4190:and 4159:Use 4153:and 4051:and 3976:beer 3968:and 3958:wort 3944:malt 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