Beta-lactamase - Knowledge

624: 2052:, while B3 seems to have arisen independently, possibly before the divergence of the gram-positive and gram-negative eubacteria about two billion years ago. PNGM-1 (Papua New Guinea Metallo-β-lactamase-1) has both metallo-β-lactamase (MBL) and tRNase Z activities, suggesting that PNGM-1 is thought to have evolved from a tRNase Z, and that the B3 MBL activity of PNGM-1 is a promiscuous activity and subclass B3 MBLs are thought to have evolved through PNGM-1 activity. Subclasses B1 and B3 has been further subdivided. 418: 1108:

Single amino acid substitutions at positions 104, 164, 238, and 240 produce the ESBL phenotype, but ESBLs with the broadest spectrum usually have more than a single amino acid substitution. Based upon different combinations of changes, currently 140 TEM-type enzymes have been described. TEM-10, TEM-12, and TEM-26 are among the most common in the United States. The term TEM comes from the name of the Athenian patient (Temoniera) from which the isolate was recovered in 1963.

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these enzymes. An increasing number of ESBLs not of TEM or SHV lineage have recently been described. The ESBLs are frequently plasmid encoded. Plasmids responsible for ESBL production frequently carry genes encoding resistance to other drug classes (for example, aminoglycosides). Therefore, antibiotic options in the treatment of ESBL-producing organisms are extremely limited.

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prevalence of ESBL-producing bacteria have been gradually increasing in acute care hospitals. The prevalence in the general population varies between countries, e.g. approximately 6% in Germany and France, 13% in Saudi Arabia, and 63% in Egypt. ESBLs are beta-lactamases that hydrolyze extended-spectrum cephalosporins with an oxyimino side chain. These cephalosporins include

1174:. Detected in the 1980s they have since the early 2000s spread and are the now the predominant ESBL type in the world. They are generally clustred into five groups based on sequencing homologies; CTX-M-1, CTX-M-2, CTX-M-8, CTX-M-9 and CTX-M-25. CTX-M-15 (belonging to the CTX-M-1 cluster) is the most prevalent CTX-M-gene. An example of beta-lactamase CTX-M-15, along with IS 284: 1705:) are not hydrolyzed by majority of ESBLs, but are hydrolyzed by associated AmpC-type β-lactamase. Also, β-lactam/β-lactamase inhibitor combinations may not be effective against organisms that produce AmpC-type β-lactamase. Sometimes these strains decrease the expression of outer membrane proteins, rendering them resistant to cephamycins. 1531:, and the high MICs seen for some Acinetobacter hosts (>64 mg/L) may reflect secondary mechanisms. They are sometimes augmented in clinical isolates by additional resistance mechanisms, such as impermeability or efflux. OXA carbapenemases also tend to have a reduced hydrolytic efficiency towards penicillins and cephalosporins. 1519:

inhibitors. The VIM enzymes are among the most widely distributed MBLs, with >40 VIM variants having been reported. Biochemical and biophysical studies revealed that VIM variants have only small variations in their kinetic parameters but substantial differences in their thermal stabilities and inhibition profiles.

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Drug Industry Antitrust Act: Hearings Before the Subcommittee on Antitrust and Monopoly of the Committee on the Judiciary, United States Senate, Eighty-seventh Congress, First [-second] Session, Pursuant to S. Res. 52 on S. 1552, a Bill to Amend and Supplement the Antitrust Laws, with Respect

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and at a limited number of geographic sites. PER-1 in isolates in Turkey, France, and Italy; VEB-1 and VEB-2 in strains from Southeast Asia; and GES-1, GES-2, and IBC-2 in isolates from South Africa, France, and Greece. PER-1 is also common in multiresistant acinetobacter species in Korea and Turkey.

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to these antibiotics and related oxyimino-beta lactams. In typical circumstances, they derive from genes for TEM-1, TEM-2, or SHV-1 by mutations that alter the amino acid configuration around the active site of these β-lactamases. A broader set of β-lactam antibiotics are susceptible to hydrolysis by

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substitutions (KPC-1 was re-sequenced in 2008 and found to be 100% homologous to published sequences of KPC-2). KPC-1 was found in North Carolina, KPC-2 in Baltimore and KPC-3 in New York. They have only 45% homology with SME and NMC/IMI enzymes and, unlike them, can be encoded by self-transmissible

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but is not usually inducible, although it can be hyperexpressed. AmpC type β-lactamases may also be carried on plasmids. AmpC β-lactamases, in contrast to ESBLs, hydrolyse broad and extended-spectrum cephalosporins (cephamycins as well as to oxyimino-β-lactams) but are not typically inhibited by the

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However, recent additions to this family show some degree of homology to one or more of the existing members of the OXA beta-lactamase family. Some confer resistance predominantly to ceftazidime, but OXA-17 confers greater resistance to cefotaxime and cefepime than it does resistance to ceftazidime.

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species, a group of rarely pathogenic commensal organisms. These enzymes are not very closely related to TEM or SHV beta-lactamases in that they show only approximately 40% identity with these two commonly isolated beta-lactamases. More than 172 CTX-M enzymes are currently known. Despite their name,

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involved in cell wall biosynthesis, and as such are one of the main targets of beta-lactam antibiotics. These three classes show undetectable sequence similarity with each other, but can still be compared using structural homology. Groups A and D are sister taxa and group C diverged before A and D.

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Amino acid sequence diversity is up to 10% in the VIM family, 15% in the IMP family, and 70% between VIM and IMP. Enzymes of both the families, nevertheless, are similar. Both are integron-associated, sometimes within plasmids. Both hydrolyse all β-lactams except monobactams, and evade all β-lactam

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Carbapenems are famously stable to AmpC β-lactamases and extended-spectrum-β-lactamases. Carbapenemases are a diverse group of β-lactamases that are active not only against the oxyimino-cephalosporins and cephamycins but also against the carbapenems. Aztreonam is stable to the metallo-β-lactamases,

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Although the inhibitor-resistant β-lactamases are not ESBLs, they are often discussed with ESBLs because they are also derivatives of the classical TEM- or SHV-type enzymes. These enzymes were at first given the designation IRT for inhibitor-resistant TEM β-lactamase; however, all have subsequently

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and is responsible for up to 20% of the plasmid-mediated ampicillin resistance in this species. ESBLs in this family also have amino acid changes around the active site, most commonly at positions 238 or 238 and 240. More than 60 SHV varieties are known. SHV-5 and SHV-12 are among the most common.

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Members of this family commonly express β-lactamases (e.g., TEM-3, TEM-4, and SHV-2 ) which confer resistance to expanded-spectrum (extended-spectrum) cephalosporins. In the mid-1980s, this new group of enzymes, the extended-spectrum β-lactamases (ESBLs), was detected (first detected in 1979). The

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The SBLs are similar in structure and mechanistically to the β-lactam target penicillin-binding proteins (PBPs) which are necessary for cell wall building and modifying. SBLs and PBPs both covalently change an active site serine residue. The difference between the PBPs and SBLs is that the latter

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from India and Pakistan. As of mid-2010, NDM-1 carrying bacteria have been introduced to other countries (including the United States and UK), most probably due to the large number of tourists travelling the globe, who may have picked up the strain from the environment, as strains containing the

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phenotype cluster around the active site of the enzyme and change its configuration, allowing access to oxyimino-beta-lactam substrates. Opening the active site to beta-lactam substrates also typically enhances the susceptibility of the enzyme to β-lactamase inhibitors, such as clavulanic acid.

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isolates from Turkey and France. The OXA beta-lactamase family was originally created as a phenotypic rather than a genotypic group for a few beta-lactamases that had a specific hydrolysis profile. Therefore, there is as little as 20% sequence homology among some of the members of this family.

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In 1957, amid concern about allergic reactions to penicillin-containing antibiotics, a beta-lactamase was sold as an antidote under the brand name neutrapen. It was theorized that the breakdown of penicillin by the enzyme would treat the allergic reaction. While it was not useful in acute

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and joint pain suspected to be caused by penicillin allergy. Its use was proposed in pediatric cases where penicillin allergy was discovered upon administration of the polio vaccine, which used penicillin as a preservative. However, some patients developed allergies to neutrapen. The

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Nicolas-Chanoine MH, Gruson C, Bialek-Davenet S, Bertrand X, Thomas-Jean F, Bert F, et al. (March 2013). "10-Fold increase (2006-11) in the rate of healthy subjects with extended-spectrum β-lactamase-producing Escherichia coli faecal carriage in a Parisian check-up centre".

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A second growing family of carbapenemases, the VIM family, was reported from Italy in 1999 and now includes 10 members, which have a wide geographic distribution in Europe, South America, and the Far East and have been found in the United States. VIM-1 was discovered in

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removed it from its formulary in 1960, only two years after adding it, citing lack of use. Some researchers continued to use it in experiments on penicillin resistance as late as 1972. It was voluntarily withdrawn from the American market by 3M Pharmaceuticals in 1997.

1881:-type carbapenemases usually remain susceptible. Resistance to non-beta-lactam antibiotics is common in strains making any of these enzymes, such that alternative options for non-beta-lactam therapy need to be determined by direct susceptibility testing. Resistance to 3774:"NEW DRUG FIGHTS ILLS OF PENICILLIN; Antibiotics Expert Finds Neutrapen Effective on Injection Side Effect ALLERGY RISE STUDIED U.S. Aide Reports Increase in Reaction to Penicillin and Like Substances Severe Reactions Few Some Severe Reactions (Published 1957)" 803:

The MBLs use the Zn ions to activate a binding site water molecule for the hydrolysis of the β-lactam ring. Zinc chelators have recently been investigated as metallo-β-lactamase inhibitors, as they are often able to restore carbapenem susceptibility.

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AmpC type β-lactamases are commonly isolated from extended-spectrum cephalosporin-resistant gram-negative bacteria. AmpC β-lactamases (also termed class C or group 1) are typically encoded on the chromosome of many gram-negative bacteria including

831:(which are gram-negative) even before penicillin entered clinical use, but penicillinase production quickly spread to bacteria that previously did not produce it or produced it only rarely. Penicillinase-resistant beta-lactams such as 1661:

susceptibility. Once an ESBL-producing strain is detected, the laboratory should report it as "resistant" to all penicillins, cephalosporins, and aztreonam, even if it is tested (in vitro) as susceptible. Associated resistance to

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and related anti-staphylococcal penicillins. These beta-lactamases differ from the TEM and SHV enzymes in that they belong to molecular class D and functional group 2d. The OXA-type beta-lactamases confer resistance to

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isolates, but fewer produce the enzyme since expression demands appropriate migration of an insertion sequence. CcrA was known before imipenem was introduced, and producers have shown little subsequent increase.

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Plasmid-mediated IMP-type carbapenemases (IMP stands for active-on-imipenem), 19 varieties of which are currently known, became established in Japan in the 1990s both in enteric gram-negative organisms and in

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Walsh TR, Weeks J, Livermore DM, Toleman MA (May 2011). "Dissemination of NDM-1 positive bacteria in the New Delhi environment and its implications for human health: an environmental point prevalence study".

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The other type of beta-lactamase is of the metallo type ("type B"). Metallo-beta-lactamases (MBLs) need metal ion(s) (1 or 2 Zn ions) on their active site for their catalytic activities. The structure of the

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but many IMP and VIM producers are resistant, owing to other mechanisms. Carbapenemases were formerly believed to derive only from classes A, B, and D, but a class C carbapenemase has been described.

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been renamed with numerical TEM designations. There are at least 19 distinct inhibitor-resistant TEM β-lactamases. Inhibitor-resistant TEM β-lactamases have been found mainly in clinical isolates of

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A few class A enzymes, most noted the plasmid-mediated KPC enzymes, are effective carbapenemases as well. Ten variants, KPC-2 through KPC-11 are known, and they are distinguished by one or two

1392:, although resistance has been described. This is no longer a primarily European epidemiology, it is found in northern parts of America often and should be tested for with complex UTI's. 3789: 1727:

are, in general, regarded as the preferred agent for treatment of infections due to ESBL-producing organisms. Carbapenems are resistant to ESBL-mediated hydrolysis and exhibit excellent

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Among gram-negative bacteria, the emergence of resistance to extended-spectrum cephalosporins has been a major concern. It appeared initially in a limited number of bacterial species (

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in Italy in 1996; since then, VIM-2 - now the predominant variant - was found repeatedly in Europe and the Far East; VIM-3 and -4 are minor variants of VIM-2 and -1, respectively.

4721: 2943:"Extended-spectrum beta-lactamases in Klebsiella pneumoniae bloodstream isolates from seven countries: dominance and widespread prevalence of SHV- and CTX-M-type beta-lactamases" 2632:"Novel insights into pivotal risk factors for rectal carriage of extended-spectrum-β-lactamase-producing enterobacterales within the general population in Lower Saxony, Germany" 1261:

Some of these enzymes are found in Enterobacteriaceae as well, whereas other uncommon ESBLs (such as BES-1, IBC-1, SFO-1, and TLA-1) have been found only in Enterobacteriaceae.

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While ESBL-producing organisms were previously associated with hospitals and institutional care, these organisms are now increasingly found in the community. CTX-M-15-positive

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Extended spectrum beta lactamase (ESBL) screening can be performed using disk-diffusion. Cefpodoxime, ceftazidime, aztreonam, cefotaxime, and/or ceftriaxone discs are used.

932:) that could mutate to hyperproduce their chromosomal class C β-lactamase. A few years later, resistance appeared in bacterial species not naturally producing AmpC enzymes ( 376: 161: 587: 1014:

but are not affected by commercially available β-lactamase inhibitors, and can, in strains with loss of outer membrane porins, provide resistance to carbapenems.

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Lee JH, Jung HI, Jung JH, Park JS, Ahn JB, Jeong SH, et al. (2004). "Dissemination of transferable AmpC-type beta-lactamase (CMY-10) in a Korean hospital".

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can maintain inhibitory activity against this class of β-lactamases. AmpC-type β-lactamase organisms are often clinically grouped through the acronym, "SPACE":

950:) due to the production of TEM- or SHV-type ESBLs (extended spectrum beta lactamases). Characteristically, such resistance has included oxyimino- (for example 2581:"Temporal trends and risk factors for extended-spectrum beta-lactamase-producing Escherichia coli in adults with catheter-associated urinary tract infections" 3447: 1527:

The OXA group of β-lactamases occur mainly in Acinetobacter species and are divided into two clusters. OXA carbapenemases hydrolyse carbapenems very slowly

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bacteria on the left are resistant to beta-lactam antibiotics, and grow next to one antibiotic (bottom) and are less inhibited by another antibiotic (top).

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inhibit most ESBLs, but the clinical effectiveness of beta-lactam/beta-lactamase inhibitor combinations cannot be relied on consistently for therapy.

2742:"High rate of intestinal colonization with extended-spectrum-beta-lactamase-producing organisms in household contacts of infected community patients" 1760: 3173:"Novel blaCTX-M variants and genotype-phenotype correlations among clinical isolates of extended spectrum beta lactamase-producing Escherichia coli" 1786:

is common, but both drugs show an inoculum effect, with diminished susceptibility as the size of the inoculum is increased from 10 to 10 organisms.

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species. IMP enzymes spread slowly to other countries in the Far East, were reported from Europe in 1997, and have been found in Canada and Brazil.

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These serine-based enzymes, like the group B betalactamases, are of ancient origin and are theorized to have evolved about two billion years ago.

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Barlow M, Hall BG (September 2002). "Phylogenetic analysis shows that the OXA beta-lactamase genes have been on plasmids for millions of years".

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Other plasmid-mediated ESBLs, such as PER, VEB, GES, and IBC beta-lactamases, have been described but are uncommon and have been found mainly in

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The OXA group (in class D) in particular is theorized to have evolved on chromosomes and moved to plasmids on at least two separate occasions.

1420: 1147:). Rather than arising by mutation, they represent examples of plasmid acquisition of beta-lactamase genes normally found on the chromosome of 1116:

SHV-1 shares 68 percent of its amino acids with TEM-1 and has a similar overall structure. The SHV-1 beta-lactamase is most commonly found in

1103:, they are also found in other species of gram-negative bacteria with increasing frequency. The amino acid substitutions responsible for the 772:-transpeptidases to inhibit bacterial cell wall biosynthesis. Serine β-lactamases are grouped by sequence similarity into types A, C, and D. 606: 2995:"Extended-spectrum beta-lactamases in the 21st century: characterization, epidemiology, and detection of this important resistance threat" 652:

bacteria on the right are sensitive to two beta-lactam antibiotics, and do not grow in the semi-circular regions surrounding antibiotics.

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Shi C, Chen J, Kang X, Shen X, Lao X, Zheng H (August 2019). "Approaches for the discovery of metallo-β-lactamase inhibitors: A review".

3918: 1657:. Moreover, one should suspect these strains when treatment with these agents for gram-negative infections fails despite reported 714:), although carbapenems are relatively resistant to beta-lactamase. Beta-lactamase provides antibiotic resistance by breaking the 3477:"Comparison of Verona Integron-Borne Metallo-β-Lactamase (VIM) Variants Reveals Differences in Stability and Inhibition Profiles" 1002:. Chromosomal-mediated AmpC β-lactamases represent a new threat, since they confer resistance to 7-alpha-methoxy-cephalosporins ( 4985: 4232:

Hall BG, Salipante SJ, Barlow M (July 2004). "Independent origins of subgroup Bl + B2 and subgroup B3 metallo-beta-lactamases".

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Administered Prices: con't] pt.25. Administered prices in the drug industry, (Antibiotics-Appendix A). 1961. pp. 14201-15329

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OXA beta-lactamases were long recognized as a less common but also plasmid-mediated beta-lactamase variety that could hydrolyze

599: 4897: 4864: 4792: 4027: 4950: 4831: 4743: 109: 1052:-resistant) isolates have recently been reported. ESBL-producing organisms may appear susceptible to some extended-spectrum 550: 396: 181: 2891:"Patterns and mechanisms of beta-lactam resistance among isolates of Escherichia coli from hospitals in the United States" 1624:

NDM-1 gene have been found in environmental samples in India. NDM have several variants which share different properties.

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Weiss RC, Crepea SB (July 1959). "Development of sensitivity to penicillinase following its use in penicillin reaction".

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and may have evolved from it. Of the three subclasses B1, B2, and B3, B1 and B2 are theorized to have evolved about one

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are the treatment of choice for serious infections due to ESBL-producing organisms, yet carbapenem-resistant (primarily

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Berglund F, Johnning A, Larsson DG, Kristiansson E (January 2021). "An updated phylogeny of the metallo-β-lactamases".

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Nordmann P, Cuzon G, Naas T (April 2009). "The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria".

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Kader AA, Kamath KA (2009). "Faecal carriage of extended-spectrum beta-lactamase-producing bacteria in the community".

777: 3415: 781: 748: 5032: 1565:, USA. A 2010 publication indicated that KPC producing Enterobacteriaceae were becoming common in the United States. 895: 2316:"Zinc Chelators as Carbapenem Adjuvants for Metallo-β-Lactamase-Producing Bacteria: In Vitro and In Vivo Evaluation" 5333: 1602: 718:' structure. These antibiotics all have a common element in their molecular structure: a four-atom ring known as a 827:

Penicillinase was the first β-lactamase to be identified. It was first isolated by Abraham and Chain in 1940 from

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is due to the production of TEM-1. Also responsible for the ampicillin and penicillin resistance that is seen in

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confusing mix of structural and functional classifications; need explanatory paragraph on what these classes are.

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Beta-lactamases are ancient bacterial enzymes. Metallo β-lactamases ("class B") are all structurally similar to

1217:. Amino acid substitutions in OXA enzymes can also give the ESBL phenotype. While most ESBLs have been found in 4925: 2631: 1558: 544: 526: 384: 169: 5188: 796:

The two types of beta-lactamases work on the basis of the two basic mechanisms of opening the β-lactam ring.

726:, the enzyme lactamase breaks the β-lactam ring open, deactivating the molecule's antibacterial properties. 3526:"Crystal structure of the carbapenemase OXA-24 reveals insights into the mechanism of carbapenem hydrolysis" 2791:"Detection and clinical significance of extended-spectrum beta-lactamases in a tertiary-care medical center" 800:

generates free enzyme and inactive antibiotic by the very quick hydrolysis of the acyl-enzyme intermediate.

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There have been few clinical studies to define the optimal therapy for infections caused by ESBL producing

3655:"Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase" 2156: 1580: 2840:"Carbapenem-non-susceptible Enterobacteriaceae in Europe: conclusions from a meeting of national experts" 4560:"Molecular diversity of extended-spectrum β-lactamases and carbapenemases, and antimicrobial resistance" 4028:

United States Congress Senate Committee on the Judiciary Subcommittee on Antitrust and Monopoly (1957).

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Symanzik C, Hillenbrand J, Stasielowicz L, Greie JC, Friedrich AW, Pulz M, et al. (December 2021).

611: 5303: 4887: 3287:"Resistance determinants and mobile genetic elements of an NDM-1-encoding Klebsiella pneumoniae strain" 2063: 519: 380: 165: 4094: 122: 5289: 5276: 5263: 5250: 5237: 5224: 5211: 5173: 4425:

Hall BG, Barlow M (April 2004). "Evolution of the serine beta-lactamases: past, present and future".

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Grundmann H, Livermore DM, Giske CG, Canton R, Rossolini GM, Campos J, et al. (November 2010).

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Zimmerman MC (August 1958). "Penicillinase-proved allergy to penicillin in poliomyelitis vaccine".

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Friedlaender S (April 1959). "Penicillinase in the treatment of allergic reactions to penicillin".

1040: 683: 672: 437: 2151: 1817:, thereby showing clinical resistance to the beta-lactam—beta lactamase inhibitor combinations of 547: 5085: 4804: 4382:

Hall BG, Barlow M (September 2003). "Structure-based phylogenies of the serine beta-lactamases".

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Principe L, Vecchio G, Sheehan G, Kavanagh K, Morroni G, Viaggi V, et al. (1 October 2020).

1933: 1846: 1783: 1577:. It is carried on a plasmid, pYMG-1, and is therefore transmissible to other bacterial strains. 1573:

The first class C carbapenemase was described in 2006 and was isolated from a virulent strain of

1389: 471: 4029: 3238:"Extended-spectrum β-lactamases: an update on their characteristics, epidemiology and detection" 4605:"A Structure-Based Classification of Class A β-Lactamases, a Broadly Diverse Family of Enzymes" 4011: 1994: 1282: 1241: 1070: 730: 687: 4126:"Novel method for detection of beta-lactamases by using a chromogenic cephalosporin substrate" 3475:

Makena A, Düzgün AÖ, Brem J, McDonough MA, Rydzik AM, Abboud MI, et al. (December 2015).

2532:"Emergence of resistance to cefamandole: possible role of cefoxitin-inducible beta-lactamases" 5106: 5025: 2013: 1928:

has been associated with the best outcomes in terms of survival and bacteriologic clearance.

1619: 1553: 1356:, thereby showing clinical resistance to the beta-lactam—lactamase inhibitor combinations of 1180: 836: 2941:

Paterson DL, Hujer KM, Hujer AM, Yeiser B, Bonomo MD, Rice LB, et al. (November 2003).

1869:; however, diminished porin expression can make such a strain carbapenem-resistant as well. 824:

ring. Molecular weights of the various penicillinases tend to cluster near 50 kilodaltons.

5178: 4935: 4689: 4469: 3537: 3298: 3184: 2382: 1961: 1838: 1381: 1344: 1278: 916: 910: 363: 148: 3882: 2740:

Valverde A, Grill F, Coque TM, Pintado V, Baquero F, Cantón R, et al. (August 2008).

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substrate which changes color from yellow to red upon beta-lactamase mediated hydrolysis.

507: 8: 5142: 4915: 4814: 449: 4473: 4009: 3541: 3302: 3188: 2386: 1056:. However, treatment with such antibiotics has been associated with high failure rates. 483: 5075: 4940: 4631: 4604: 4586: 4559: 4538: 4511: 4493: 4407: 4307: 4276: 4257: 4209: 4174: 4047:"Automated method for determination of penicillins, cephalosporins, and penicillinases" 3910: 3684: 3560: 3525: 3501: 3476: 3409:

isolates producing CTX-M-15 extended-spectrum β-lactamase (ESBL) in the United Kingdom"

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SME (Serratia marcescens enzymes), IMI (IMIpenem-hydrolysing β-lactamase), NMC and CcrA

1332: 1230: 1163: 442: 37: 4150: 4125: 4071: 4046: 3824: 3751: 3596: 2967: 2942: 2915: 2890: 2815: 2790: 2556: 2531: 2447: 2422: 2210: 2185: 562: 114: 5338: 4910: 4665: 4636: 4591: 4485: 4442: 4399: 4347: 4312: 4249: 4214: 4196: 4155: 4076: 3992: 3988: 3957: 3953: 3914: 3902: 3863: 3859: 3828: 3781: 3755: 3719: 3676: 3671: 3654: 3635: 3600: 3565: 3506: 3385: 3367: 3326: 3267: 3210: 3153: 3059: 3024: 3019: 2994: 2972: 2958: 2920: 2871: 2820: 2771: 2722: 2695: 2663: 2651: 2612: 2561: 2452: 2355: 2343: 2335: 2288: 2253: 2215: 2056: 1956:

therapy as a result of resistance due to porin loss. Some patients have responded to

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have failed even more often, despite the organism's susceptibility to the antibiotic

1561:) globally has been the most common carbapenemase, and was first detected in 1996 in 1338: 946: 863: 762: 538: 371: 188: 156: 4261: 3688: 3222: 2806: 2300: 2087: 623: 312: 65: 5121: 5116: 5090: 5018: 4657: 4626: 4616: 4581: 4571: 4533: 4523: 4497: 4477: 4434: 4391: 4339: 4302: 4292: 4241: 4204: 4186: 4145: 4137: 4066: 4058: 3984: 3949: 3894: 3855: 3820: 3747: 3711: 3666: 3627: 3592: 3555: 3545: 3496: 3488: 3375: 3357: 3316: 3306: 3257: 3249: 3200: 3192: 3143: 3133: 3100: 3090: 3051: 3014: 3006: 2962: 2954: 2910: 2902: 2861: 2851: 2810: 2802: 2761: 2753: 2687: 2643: 2602: 2592: 2551: 2543: 2442: 2434: 2404: 2390: 2327: 2280: 2245: 2205: 2197: 1910: 1882: 1671: 1613: 1454: 1425: 1320: 1270: 1219: 1093: 1074: 648: 359: 144: 4411: 4297: 4277:"Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo- 3010: 2201: 733:

are usually secreted, especially when antibiotics are present in the environment.

325: 78: 5168: 5152: 5065: 4369: 3811:

Hyman AL (February 1959). "Anaphylactic shock after therapy with penicillinase".

3631: 3311: 1886: 1810: 1675: 1663: 1431: 1349: 1298: 1277:

in the UK, and tend to be resistant to all oral β-lactam antibiotics, as well as

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in increasing numbers. Although TEM-type beta-lactamases are most often found in

768:, from which the enzyme is thought to have evolved. β-lactam antibiotics bind to 757: 423: 337: 90: 566: 5317: 5206: 5147: 4967: 4930: 4902: 4854: 4836: 4786: 4748: 4438: 3530:

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

3196: 2856: 2839: 2438: 2136: 2103: 1957: 1562: 1348:. Although the inhibitor-resistant TEM variants are resistant to inhibition by 1286: 1087: 582: 4576: 4481: 4395: 4245: 3883:"A New Concept in the Treatment of Penicillin Reactions: Use of Penicillinase" 2597: 2249: 1505: 5327: 5111: 5070: 4994: 4920: 4869: 4200: 3906: 3785: 3371: 3362: 3253: 3138: 2339: 2186:"Effect of beta-lactamase location in Escherichia coli on penicillin synergy" 2030: 1974: 1965: 1809:

Although the inhibitor-resistant TEM variants are resistant to inhibition by

1711: 1498: 1458: 1326: 1256: 1235: 1225: 1118: 1099: 1081: 1053: 934: 928: 922: 695: 632: 557: 118: 4275:

Lee JH, Takahashi M, Jeon JH, Kang LW, Seki M, Park KS, et al. (2019).

4191: 3715: 3550: 2676: 2236:

Rotondo CM, Wright GD (October 2017). "Inhibitors of metallo-β-lactamases".

417: 5060: 4776: 4756: 4669: 4640: 4595: 4528: 4489: 4446: 4403: 4351: 4316: 4253: 4218: 3996: 3961: 3867: 3832: 3759: 3723: 3680: 3639: 3604: 3569: 3510: 3389: 3330: 3271: 3214: 3157: 3095: 3063: 3028: 2976: 2875: 2775: 2726: 2699: 2655: 2616: 2456: 2347: 2292: 2257: 1826: 1667: 1484: 1468: 1415: 1377: 1365: 743: 4661: 4343: 4159: 4080: 3898: 3653:

Kim JY, Jung HI, An YJ, Lee JH, Kim SJ, Jeong SH, et al. (May 2006).

3122:"A Review of SHV Extended-Spectrum β-Lactamases: Neglected Yet Ubiquitous" 2924: 2824: 2331: 2219: 2142:, "separation"), the first enzyme discovered in 1833 by Payen and Persoz. 5284: 5219: 5055: 4844: 4771: 4761: 4621: 3492: 3055: 2906: 2757: 2691: 2565: 2547: 2114: 2055:

Serine beta-lactamases (classes A, C, and D) appear to have evolved from

1945: 1937: 1866: 1862: 1834: 1830: 1822: 1818: 1753: 1749: 1724: 1694: 1679: 1637:

In general, an isolate is suspected to be an ESBL producer when it shows

1492: 1462: 1448: 1403: 1373: 1369: 1361: 1357: 1210: 1202: 1155: 1140: 1136: 1032: 1028: 1003: 995: 983: 971: 963: 959: 951: 832: 812:

Penicillinase is a specific type of β-lactamase, showing specificity for

719: 703: 636: 4141: 4062: 2866: 821: 4999: 4882: 4799: 2284: 2164: 2026: 1953: 1941: 1916: 1842: 1687: 1642: 1544: 1435: 1385: 1306: 1294: 1290: 1198: 1159: 1132: 1045: 1024: 999: 991: 955: 940: 817: 813: 723: 715: 707: 699: 691: 675: 628: 495: 3470: 3468: 2647: 260: 254: 248: 242: 236: 230: 224: 218: 212: 206: 200: 194: 5258: 5232: 4975: 4730: 3042:

Jacoby GA, Munoz-Price LS (January 2005). "The new beta-lactamases".

2500: 2470: 2395: 2370: 2008: 1925: 1814: 1702: 1698: 1683: 1654: 1650: 1646: 1608: 1522: 1439: 1353: 1302: 1206: 1193: 1049: 1036: 1011: 1007: 987: 979: 975: 967: 711: 102: 4729: 4014:

to the Manufacture and Distribution of Drugs, and for Other Purposes

2629: 5312: 4877: 4364: 4329: 4095:"Federal Register, Volume 62 Issue 229 (Friday, November 28, 1997)" 3465: 2131: 2083: 1979: 1969: 1929: 1921: 1798: 1779: 1716: 1444: 1409: 1274: 1149: 1144: 752: 679: 332: 85: 4123: 1596: 4819: 4010:

United States Congress Senate Committee on the Judiciary (1961).

2098: 2045: 1723:

stability in the presence of many ESBL/AmpC strains.) Currently,

785: 514: 97: 2889:

Cooksey R, Swenson J, Clark N, Gay E, Thornsberry C (May 1990).

1678:

resistance, creates problems. Beta-lactamase inhibitors such as

1205:

and are characterized by their high hydrolytic activity against

5271: 5041: 4766: 2092: 1653:) but resistance to the third-generation cephalosporins and to 668: 594: 490: 478: 466: 391: 176: 30: 4124:

O'Callaghan CH, Morris A, Kirby SM, Shingler AH (April 1972).

3880: 2313: 1534: 643: 5245: 4945: 2837: 2119: 1131:

These enzymes were named for their greater activity against

1104: 4809: 4781: 3285:

Hudson CM, Bent ZW, Meagher RJ, Williams KP (7 June 2014).

3119: 2125: 2079: 2007:

anaphylactic shock, it showed positive results in cases of

1506:

VIM (Verona integron-encoded metallo-β-lactamase) (Class B)

1184:

ATCC BAA-2146. The initials stand for "Cefotaxime-Munich".

1178:, has been found to have transposed onto the chromosome of 502: 353: 319: 307: 138: 72: 60: 5010: 4175:"Extended-spectrum ß-lactamases in gram negative bacteria" 3736: 3523: 3120:

Liakopoulos A, Mevius D, Ceccarelli D (5 September 2016).

1709:

studies have yielded mixed results against ESBL-producing

1017: 3474: 3284: 3171:

Ramadan AA, Abdelaziz NA, Amin MA, Aziz RK (March 2019).

2739: 2049: 1069:

TEM-1 is the most commonly encountered beta-lactamase in

4648:

Yoon EJ, Jeong SH (March 2021). "Class D β-lactamases".

3446:. Food and Drug Administration (FDA). 18 February 2015. 3343: 3170: 2940: 2025:

Beta-lactamase enzymatic activity can be detected using

1627: 1485:

IMP-type carbapenemases (metallo-β-lactamases) (class B)

288:

Metallo-beta-lactamase L1 homotetramer, Stenotrophomonas

4602: 3524:

Santillana E, Beceiro A, Bou G, Romero A (March 2007).

2578: 1585:

In general, these are of little clinical significance.

842: 283: 4603:

Philippon A, Slama P, Dény P, Labia R (January 2016).

2888: 1719:, a fourth-generation cephalosporin, has demonstrated 1123:

The initials stand for "sulfhydryl reagent variable".

5301: 1804: 4557: 4274: 3441:"Clinical Review, NDA 206494, Ceftazidime-avibactam" 2420: 2371:"An enzyme from bacteria able to destroy penicillin" 1801:

on testing, despite the use of a standard inoculum.

1384:, they normally remain susceptible to inhibition by 4231: 1395: 1312: 4684: 4044: 1857:AmpC-producing strains are typically resistant to 1523:OXA (oxacillinase) group of β-lactamases (class D) 1135:than other oxyimino-beta-lactam substrates (e.g., 1126: 3881:American Academy of Pediatrics (1 October 1958). 3618:Cuzon G, Naas T, Nordmann P (February 2010). "". 3617: 3582: 3041: 1897: 5325: 4558:Sawa T, Kooguchi K, Moriyama K (December 2020). 4281:-lactamases: a molecular and evolutionary study" 3402: 2421:Philippon A, Arlet G, Jacoby GA (January 2002). 1748:Strains producing only ESBLs are susceptible to 1187: 1111: 1064: 3701: 2988: 2986: 2936: 2934: 2579:Spadafino JT, Cohen B, Liu J, Larson E (2014). 2270: 1674:, as well as high frequency of co-existence of 1597:NDM-1 (New Delhi metallo-β-lactamase) (class B) 1233:, the OXA-type ESBLs have been found mainly in 1213:and the fact that they are poorly inhibited by 2831: 2585:Antimicrobial Resistance and Infection Control 2529: 2423:"Plasmid-determined AmpC-type beta-lactamases" 2416: 2414: 5026: 4715: 3403:Woodford N, Ward E, Kaufmann ME, et al. 3396: 3344:Cantón R, González-Alba JM, Galán JC (2012). 2788: 2235: 1952:. Several reports have documented failure of 1162:. They are widely described among species of 4418: 3845: 3730: 3695: 3652: 3646: 3611: 3576: 3517: 3035: 2983: 2931: 2368: 1588:CcrA (CfiA). Its gene occurs in ca. 1–3% of 835:were developed, but there is now widespread 788:, from which it is thought to have evolved. 4117: 4045:Lindström EB, Nordström K (February 1972). 3974: 3942:Journal of the American Medical Association 3813:Journal of the American Medical Association 3235: 2882: 2782: 2712: 2411: 1972:for bacteremia involving an ESBL-producing 1841:, they remain susceptible to inhibition by 1239:. OXA-type ESBLs have been found mainly in 970:), but not 7-alpha-methoxy-cephalosporins ( 5033: 5019: 4722: 4708: 4459: 4453: 4424: 4381: 3414:. Health Protection Agency. Archived from 2177: 2001: 982:); has been blocked by inhibitors such as 4692:at the U.S. National Library of Medicine 4650:The Journal of Antimicrobial Chemotherapy 4647: 4630: 4620: 4585: 4575: 4537: 4527: 4332:The Journal of Antimicrobial Chemotherapy 4306: 4296: 4208: 4190: 4172: 4149: 4070: 3939: 3670: 3559: 3549: 3500: 3379: 3361: 3320: 3310: 3261: 3204: 3147: 3137: 3104: 3094: 3018: 2966: 2914: 2865: 2855: 2814: 2765: 2680:The Journal of Antimicrobial Chemotherapy 2606: 2596: 2555: 2523: 2446: 2394: 2209: 1985: 896:Learn how and when to remove this message 4375: 4225: 2992: 2129:, indicating an enzyme, is derived from 1964:therapy, but, in a recent comparison of 1908:For infections caused by ESBL-producing 1611:in 2009, this gene is now widespread in 1419:species where its expression is usually 1073:. Up to 90% of ampicillin resistance in 642: 622: 1892: 1105:extended-spectrum beta lactamase (ESBL) 1018:Extended-spectrum beta-lactamase (ESBL) 5326: 3921:from the original on 28 September 2018 791: 747:serine β-lactamase (SBLs) is given by 5014: 4951:Activation-induced cytidine deaminase 4703: 4179:Journal of Global Infectious Diseases 4130:Antimicrobial Agents and Chemotherapy 4051:Antimicrobial Agents and Chemotherapy 3810: 3481:Antimicrobial Agents and Chemotherapy 3453:from the original on 28 February 2017 3346:"CTX-M Enzymes: Origin and Diffusion" 3242:Journal of Antimicrobial Chemotherapy 2947:Antimicrobial Agents and Chemotherapy 2895:Antimicrobial Agents and Chemotherapy 2789:Emery CL, Weymouth LA (August 1997). 2536:Antimicrobial Agents and Chemotherapy 2511:from the original on 11 February 2022 2501:"Ambler class A beta-lactamases: SHV" 2481:from the original on 11 February 2022 2471:"Ambler class A beta-lactamases: TEM" 2427:Antimicrobial Agents and Chemotherapy 1738: 1628:Treatment of ESBL/AmpC/carbapenemases 1035:, as well as the oxyimino-monobactam 966:, as well as the oxyimino-monobactam 4105:from the original on 23 October 2023 3792:from the original on 31 January 2022 3076: 2715:Eastern Mediterranean Health Journal 2530:Sanders CC, Sanders WE (June 1979). 2231: 2229: 1845:and subsequently the combination of 1388:and subsequently the combination of 846: 843:Resistance in gram-negative bacteria 3044:The New England Journal of Medicine 2183: 2117:was isolated from soured milk) and 1872: 1632: 13: 4550: 4285:Emerging Microbes & Infections 4034:. U.S. Government Printing Office. 4017:. U.S. Government Printing Office. 3236:Castanheira M (3 September 2021). 2273:Chemical Biology & Drug Design 2090:on the second carbon in the ring. 1273:are a cause of community-acquired 778:New Delhi metallo-beta-lactamase 1 14: 5355: 4678: 3825:10.1001/jama.1959.73000230003011a 2226: 1551:As of February 2009, the class A 1475: 5311: 3954:10.1001/jama.1958.02990320001001 3672:10.1111/j.1365-2958.2006.05146.x 3005:(4): 933–51, table of contents. 2959:10.1128/AAC.47.11.3554-3560.2003 2795:Journal of Clinical Microbiology 2746:Journal of Clinical Microbiology 1805:Inhibitor-resistant β-lactamases 1603:New Delhi metallo-beta-lactamase 1568: 1396:AmpC-type β-lactamases (class C) 1313:Inhibitor-resistant β-lactamases 1285:. Treatment options may include 851: 807: 416: 282: 29: 4733:: carbon-nitrogen non-peptide ( 4504: 4358: 4323: 4268: 4166: 4087: 4038: 4021: 4003: 3968: 3933: 3874: 3839: 3804: 3766: 3740:The Lancet. Infectious Diseases 3585:The Lancet. Infectious Diseases 3433: 3405:"Molecular characterisation of 3337: 3278: 3229: 3164: 3113: 3070: 2807:10.1128/JCM.35.8.2061-2067.1997 2733: 2706: 2670: 2636:Journal of Applied Microbiology 2623: 2572: 2238:Current Opinion in Microbiology 1127:CTX-M beta-lactamases (class A) 4926:Inosine monophosphate synthase 4462:Journal of Molecular Evolution 4384:Journal of Molecular Evolution 4234:Journal of Molecular Evolution 2505:Beta-Lactamase DataBase (BLDB) 2493: 2463: 2362: 2307: 2264: 1301:. In desperation, once-daily 1: 4609:Clinical Microbiology Reviews 4298:10.1080/22221751.2019.1692638 3752:10.1016/S1473-3099(11)70059-7 3597:10.1016/S1473-3099(09)70054-4 3011:10.1128/CMR.14.4.933-951.2001 2999:Clinical Microbiology Reviews 2475:Beta-Lactamase DataBase (BLDB 2202:10.1128/AEM.17.6.783-786.1969 2170: 1797:-type ESBLs are resistant to 1309:injections may also be used. 1188:OXA beta-lactamases (class D) 1112:SHV beta-lactamases (class A) 1065:TEM beta-lactamases (class A) 348:Available protein structures: 133:Available protein structures: 4516:Emerging Infectious Diseases 3989:10.1016/0021-8707(59)90041-3 3860:10.1016/0021-8707(59)90087-5 3632:10.1016/j.patbio.2009.07.026 3312:10.1371/journal.pone.0099209 3083:Emerging Infectious Diseases 2993:Bradford PA (October 2001). 2369:Abraham EP, Chain E (1940). 2073: 2039: 2020: 1982:produced the better outcome 1731:activity against strains of 1264: 736: 729:Beta-lactamases produced by 7: 5040: 2145: 2064:penicillin-binding proteins 1936:have been less successful. 1324:, but also some strains of 871:. The specific problem is: 10: 5360: 5344:Enzymes of known structure 4888:Protein-arginine deiminase 4810:Fatty acid amide hydrolase 4439:10.1016/j.drup.2004.02.003 3197:10.1038/s41598-019-39730-0 2857:10.2807/ese.15.46.19711-en 2439:10.1128/AAC.46.1.1-11.2002 1607:Originally described from 1600: 422:Action of β-lactamase and 5197: 5189:Michaelis–Menten kinetics 5161: 5130: 5099: 5048: 4984: 4961: 4896: 4863: 4830: 4742: 4577:10.1186/s40560-020-0429-6 4564:Journal of Intensive Care 4512:"Etymologia: β-Lactamase" 4482:10.1007/s00239-002-2328-y 4396:10.1007/s00239-003-2473-y 4246:10.1007/s00239-003-2572-9 3704:Microbial Drug Resistance 3350:Frontiers in Microbiology 3126:Frontiers in Microbiology 2598:10.1186/s13756-014-0039-y 2320:Microbial Drug Resistance 2250:10.1016/j.mib.2017.10.026 1249: 1154:a few are more active on 722:(β-lactam) ring. Through 605: 593: 581: 576: 572: 556: 537: 525: 513: 501: 489: 477: 465: 460: 448: 436: 431: 415: 410: 390: 370: 352: 347: 343: 331: 318: 306: 298: 293: 281: 276: 187: 175: 155: 137: 132: 128: 108: 96: 84: 71: 59: 51: 46: 28: 23: 5081:Diffusion-limited enzyme 4694:Medical Subject Headings 4173:Rawat D, Nair D (2010). 3363:10.3389/fmicb.2012.00110 3139:10.3389/fmicb.2016.01374 1920:species, treatment with 1766:For organisms producing 1743: 1539:carbapenemase) (class A) 1059: 5334:Beta-lactam antibiotics 4805:Aspartylglucosaminidase 4685:Beta-lactamase database 4427:Drug Resistance Updates 4192:10.4103/0974-777X.68531 3716:10.1089/mdr.2004.10.224 3551:10.1073/pnas.0607557104 2002:Use as a pharmaceutical 1934:piperacillin/tazobactam 1865:and are susceptible to 1852: 1847:piperacillin/tazobactam 1784:piperacillin/tazobactam 1759:and show little if any 1430:β-lactamase inhibitors 1423:; it may also occur on 1390:piperacillin/tazobactam 751:. The alpha-beta fold ( 688:beta-lactam antibiotics 4529:10.3201/eid2209.ET2209 4522:(9): 1689–1631. 2016. 3659:Molecular Microbiology 3254:10.1093/jacamr/dlab092 3096:10.3201/eid2404.et2404 1995:Pseudomonas aeruginosa 1987:Pseudomonas aeruginosa 1641:susceptibility to the 1575:Enterobacter aerogenes 1242:Pseudomonas aeruginosa 1071:gram-negative bacteria 761:) resembles that of a 731:gram-negative bacteria 657: 640: 277:Metallo-beta-lactamase 5174:Eadie–Hofstee diagram 5107:Allosteric regulation 3899:10.1542/peds.22.4.658 2332:10.1089/mdr.2020.0037 2152:β-lactamase inhibitor 1859:oxyimino-beta lactams 1774:type ESBLs, apparent 1620:Klebsiella pneumoniae 1554:Klebsiella pneumoniae 1181:Klebsiella pneumoniae 646: 626: 24:Serine beta-lactamase 5184:Lineweaver–Burk plot 4936:GTP cyclohydrolase I 4622:10.1128/CMR.00019-15 3493:10.1128/AAC.01768-15 3056:10.1056/NEJMra041359 2907:10.1128/AAC.34.5.739 2758:10.1128/JCM.01008-08 2548:10.1128/AAC.15.6.792 2190:Applied Microbiology 2184:Neu HC (June 1969). 1893:According to species 1889:is especially high. 1839:ampicillin/sulbactam 1382:ampicillin/sulbactam 1345:Citrobacter freundii 1039:. Thus ESBLs confer 994:and did not involve 878:improve this section 867:to meet Knowledge's 4916:Adenosine deaminase 4815:Histone deacetylase 4662:10.1093/jac/dkaa513 4474:2002JMolE..55..314B 4344:10.1093/jac/dkaa392 4142:10.1128/AAC.1.4.283 4063:10.1128/aac.1.2.100 3620:Pathologie-Biologie 3542:2007PNAS..104.5354S 3303:2014PLoSO...999209H 3189:2019NatSR...9.4224R 2387:1940Natur.146..837A 1879:IMP-, VIM-, and OXA 1763:with these agents. 792:Mechanism of action 741:The structure of a 426:of the intermediate 5143:Enzyme superfamily 5076:Enzyme promiscuity 4941:Cytidine deaminase 4900:: Cyclic amidines/ 4867:: Linear amidines/ 3977:Journal of Allergy 3848:Journal of Allergy 3780:. 4 October 1957. 3778:The New York Times 3177:Scientific Reports 2692:10.1093/jac/dks429 2285:10.1111/cbdd.13526 1789:Strains with some 1739:According to genes 1735:expressing ESBLs. 1733:Enterobacteriaceae 1333:Klebsiella oxytoca 1275:urinary infections 1231:Enterobacteriaceae 1164:Enterobacteriaceae 974:; in other words, 658: 641: 627:Core structure of 55:β-lactamase domain 38:Streptomyces albus 5299: 5298: 5008: 5007: 4911:Guanine deaminase 4746:: Linear amides / 3079:"Etymologia: TEM" 2844:Euro Surveillance 2648:10.1111/jam.15399 2326:(10): 1133–1143. 2059: 2050:billion years ago 906: 905: 898: 869:quality standards 860:This section may 784:. It resembles a 771: 765: 621: 620: 617: 616: 520:metabolic pathway 406: 405: 402: 401: 397:structure summary 272: 271: 268: 267: 182:structure summary 5351: 5316: 5315: 5307: 5179:Hanes–Woolf plot 5122:Enzyme activator 5117:Enzyme inhibitor 5091:Enzyme catalysis 5035: 5028: 5021: 5012: 5011: 4834:: Cyclic amides/ 4724: 4717: 4710: 4701: 4700: 4673: 4644: 4634: 4624: 4599: 4589: 4579: 4544: 4543: 4541: 4531: 4508: 4502: 4501: 4457: 4451: 4450: 4422: 4416: 4415: 4379: 4373: 4362: 4356: 4355: 4327: 4321: 4320: 4310: 4300: 4291:(1): 1688–1700. 4272: 4266: 4265: 4229: 4223: 4222: 4212: 4194: 4170: 4164: 4163: 4153: 4121: 4115: 4114: 4112: 4110: 4091: 4085: 4084: 4074: 4042: 4036: 4035: 4025: 4019: 4018: 4007: 4001: 4000: 3972: 3966: 3965: 3937: 3931: 3930: 3928: 3926: 3878: 3872: 3871: 3843: 3837: 3836: 3808: 3802: 3801: 3799: 3797: 3770: 3764: 3763: 3734: 3728: 3727: 3699: 3693: 3692: 3674: 3650: 3644: 3643: 3615: 3609: 3608: 3580: 3574: 3573: 3563: 3553: 3521: 3515: 3514: 3504: 3472: 3463: 3462: 3460: 3458: 3452: 3445: 3437: 3431: 3430: 3428: 3426: 3420: 3413: 3407:Escherichia coli 3400: 3394: 3393: 3383: 3365: 3341: 3335: 3334: 3324: 3314: 3282: 3276: 3275: 3265: 3233: 3227: 3226: 3208: 3168: 3162: 3161: 3151: 3141: 3117: 3111: 3110: 3108: 3098: 3074: 3068: 3067: 3039: 3033: 3032: 3022: 2990: 2981: 2980: 2970: 2938: 2929: 2928: 2918: 2886: 2880: 2879: 2869: 2859: 2835: 2829: 2828: 2818: 2801:(8): 2061–2067. 2786: 2780: 2779: 2769: 2752:(8): 2796–2799. 2737: 2731: 2730: 2721:(6): 1365–1370. 2710: 2704: 2703: 2674: 2668: 2667: 2642:(4): 3256–3264. 2627: 2621: 2620: 2610: 2600: 2576: 2570: 2569: 2559: 2527: 2521: 2520: 2518: 2516: 2497: 2491: 2490: 2488: 2486: 2467: 2461: 2460: 2450: 2418: 2409: 2408: 2398: 2396:10.1038/146837a0 2366: 2360: 2359: 2311: 2305: 2304: 2279:(2): 1427–1440. 2268: 2262: 2261: 2233: 2224: 2223: 2213: 2181: 2082:) refers to the 2060:-transpeptidases 2057: 2029:, a chromogenic 1911:Escherichia coli 1899:Escherichia coli 1883:fluoroquinolones 1672:sulfamethoxazole 1633:General overview 1614:Escherichia coli 1426:Escherichia coli 1041:multi-resistance 901: 894: 890: 887: 881: 855: 854: 847: 769: 763: 684:multi-resistance 649:Escherichia coli 574: 573: 420: 408: 407: 345: 344: 286: 274: 273: 263: 257: 251: 245: 239: 233: 227: 221: 215: 209: 203: 197: 130: 129: 33: 21: 20: 16:Class of enzymes 5359: 5358: 5354: 5353: 5352: 5350: 5349: 5348: 5324: 5323: 5322: 5310: 5302: 5300: 5295: 5207:Oxidoreductases 5193: 5169:Enzyme kinetics 5157: 5153:List of enzymes 5126: 5095: 5066:Catalytic triad 5044: 5039: 5009: 5004: 4980: 4968:Aminohydrolases 4966: 4957: 4903:Aminohydrolases 4901: 4892: 4868: 4859: 4837:Amidohydrolases 4835: 4826: 4749:Amidohydrolases 4747: 4738: 4728: 4690:beta-Lactamases 4681: 4676: 4553: 4551:Further reading 4548: 4547: 4510: 4509: 4505: 4458: 4454: 4423: 4419: 4380: 4376: 4363: 4359: 4328: 4324: 4273: 4269: 4230: 4226: 4171: 4167: 4122: 4118: 4108: 4106: 4099:www.govinfo.gov 4093: 4092: 4088: 4043: 4039: 4026: 4022: 4008: 4004: 3973: 3969: 3938: 3934: 3924: 3922: 3879: 3875: 3844: 3840: 3809: 3805: 3795: 3793: 3772: 3771: 3767: 3735: 3731: 3700: 3696: 3651: 3647: 3616: 3612: 3581: 3577: 3522: 3518: 3473: 3466: 3456: 3454: 3450: 3443: 3439: 3438: 3434: 3424: 3422: 3421:on 15 June 2007 3418: 3411: 3401: 3397: 3342: 3338: 3283: 3279: 3234: 3230: 3169: 3165: 3118: 3114: 3077:Ruiz J (2018). 3075: 3071: 3040: 3036: 2991: 2984: 2953:(11): 3554–60. 2939: 2932: 2887: 2883: 2836: 2832: 2787: 2783: 2738: 2734: 2711: 2707: 2675: 2671: 2628: 2624: 2577: 2573: 2528: 2524: 2514: 2512: 2499: 2498: 2494: 2484: 2482: 2469: 2468: 2464: 2419: 2412: 2367: 2363: 2312: 2308: 2269: 2265: 2234: 2227: 2182: 2178: 2173: 2157:ESBL-producing 2148: 2076: 2042: 2023: 2014:Albany Hospital 2004: 1990: 1906: 1895: 1887:aminoglycosides 1875: 1855: 1811:clavulanic acid 1807: 1778:sensitivity to 1761:inoculum effect 1746: 1741: 1676:fluoroquinolone 1664:aminoglycosides 1635: 1630: 1605: 1599: 1583: 1571: 1557:carbapenemase ( 1541: 1525: 1508: 1487: 1478: 1432:clavulanic acid 1398: 1350:clavulanic acid 1315: 1299:chloramphenicol 1267: 1252: 1215:clavulanic acid 1190: 1129: 1114: 1067: 1062: 1020: 902: 891: 885: 882: 875: 856: 852: 845: 839:to even these. 810: 794: 766:-transpeptidase 739: 661:Beta-lactamases 427: 424:decarboxylation 289: 259: 253: 247: 241: 235: 229: 223: 217: 211: 205: 199: 193: 42: 17: 12: 11: 5: 5357: 5347: 5346: 5341: 5336: 5321: 5320: 5297: 5296: 5294: 5293: 5280: 5267: 5254: 5241: 5228: 5215: 5201: 5199: 5195: 5194: 5192: 5191: 5186: 5181: 5176: 5171: 5165: 5163: 5159: 5158: 5156: 5155: 5150: 5145: 5140: 5134: 5132: 5131:Classification 5128: 5127: 5125: 5124: 5119: 5114: 5109: 5103: 5101: 5097: 5096: 5094: 5093: 5088: 5083: 5078: 5073: 5068: 5063: 5058: 5052: 5050: 5046: 5045: 5038: 5037: 5030: 5023: 5015: 5006: 5005: 5003: 5002: 4997: 4991: 4989: 4982: 4981: 4979: 4978: 4972: 4970: 4959: 4958: 4956: 4955: 4954: 4953: 4948: 4938: 4933: 4931:DCMP deaminase 4928: 4923: 4918: 4913: 4907: 4905: 4894: 4893: 4891: 4890: 4885: 4880: 4874: 4872: 4870:Ureohydrolases 4861: 4860: 4858: 4857: 4855:Dihydroorotase 4852: 4850:Beta-lactamase 4847: 4841: 4839: 4828: 4827: 4825: 4824: 4823: 4822: 4812: 4807: 4802: 4797: 4796: 4795: 4790: 4787:Aspartoacylase 4784: 4774: 4769: 4764: 4759: 4753: 4751: 4740: 4739: 4727: 4726: 4719: 4712: 4704: 4698: 4697: 4687: 4680: 4679:External links 4677: 4675: 4674: 4656:(4): 836–864. 4645: 4600: 4554: 4552: 4549: 4546: 4545: 4503: 4452: 4417: 4374: 4357: 4338:(1): 117–123. 4322: 4267: 4224: 4185:(3): 263–274. 4165: 4116: 4086: 4037: 4020: 4002: 3967: 3948:(15): 1807–9. 3932: 3873: 3838: 3803: 3765: 3729: 3694: 3645: 3610: 3575: 3536:(13): 5354–9. 3516: 3487:(3): 1377–84. 3464: 3432: 3395: 3336: 3277: 3248:(3): dlab092. 3228: 3163: 3112: 3069: 3034: 2982: 2930: 2881: 2830: 2781: 2732: 2705: 2686:(3): 562–568. 2669: 2622: 2571: 2542:(6): 792–797. 2522: 2492: 2462: 2410: 2361: 2306: 2263: 2225: 2175: 2174: 2172: 2169: 2168: 2167: 2162: 2154: 2147: 2144: 2096:is a blend of 2075: 2072: 2041: 2038: 2022: 2019: 2003: 2000: 1989: 1984: 1958:aminoglycoside 1905: 1896: 1894: 1891: 1874: 1873:Carbapenemases 1871: 1854: 1851: 1806: 1803: 1745: 1742: 1740: 1737: 1634: 1631: 1629: 1626: 1601:Main article: 1598: 1595: 1582: 1579: 1570: 1567: 1563:North Carolina 1540: 1533: 1524: 1521: 1507: 1504: 1486: 1483: 1477: 1476:Carbapenemases 1474: 1397: 1394: 1314: 1311: 1287:nitrofurantoin 1266: 1263: 1251: 1248: 1189: 1186: 1128: 1125: 1113: 1110: 1088:N. gonorrhoeae 1066: 1063: 1061: 1058: 1054:cephalosporins 1019: 1016: 904: 903: 886:September 2021 859: 857: 850: 844: 841: 809: 806: 793: 790: 738: 735: 696:cephalosporins 678:) produced by 633:cephalosporins 619: 618: 615: 614: 609: 603: 602: 597: 591: 590: 585: 579: 578: 570: 569: 560: 554: 553: 542: 535: 534: 529: 523: 522: 517: 511: 510: 505: 499: 498: 493: 487: 486: 481: 475: 474: 469: 463: 462: 458: 457: 452: 446: 445: 440: 434: 433: 429: 428: 421: 413: 412: 404: 403: 400: 399: 394: 388: 387: 374: 368: 367: 357: 350: 349: 341: 340: 335: 329: 328: 323: 316: 315: 310: 304: 303: 300: 296: 295: 291: 290: 287: 279: 278: 270: 269: 266: 265: 191: 185: 184: 179: 173: 172: 159: 153: 152: 142: 135: 134: 126: 125: 112: 106: 105: 100: 94: 93: 88: 82: 81: 76: 69: 68: 63: 57: 56: 53: 49: 48: 44: 43: 41:beta-lactamase 34: 26: 25: 15: 9: 6: 4: 3: 2: 5356: 5345: 5342: 5340: 5337: 5335: 5332: 5331: 5329: 5319: 5314: 5309: 5308: 5305: 5291: 5287: 5286: 5281: 5278: 5274: 5273: 5268: 5265: 5261: 5260: 5255: 5252: 5248: 5247: 5242: 5239: 5235: 5234: 5229: 5226: 5222: 5221: 5216: 5213: 5209: 5208: 5203: 5202: 5200: 5196: 5190: 5187: 5185: 5182: 5180: 5177: 5175: 5172: 5170: 5167: 5166: 5164: 5160: 5154: 5151: 5149: 5148:Enzyme family 5146: 5144: 5141: 5139: 5136: 5135: 5133: 5129: 5123: 5120: 5118: 5115: 5113: 5112:Cooperativity 5110: 5108: 5105: 5104: 5102: 5098: 5092: 5089: 5087: 5084: 5082: 5079: 5077: 5074: 5072: 5071:Oxyanion hole 5069: 5067: 5064: 5062: 5059: 5057: 5054: 5053: 5051: 5047: 5043: 5036: 5031: 5029: 5024: 5022: 5017: 5016: 5013: 5001: 5000:Thiaminase II 4998: 4996: 4995:Riboflavinase 4993: 4992: 4990: 4987: 4983: 4977: 4974: 4973: 4971: 4969: 4964: 4960: 4952: 4949: 4947: 4944: 4943: 4942: 4939: 4937: 4934: 4932: 4929: 4927: 4924: 4922: 4921:AMP deaminase 4919: 4917: 4914: 4912: 4909: 4908: 4906: 4904: 4899: 4895: 4889: 4886: 4884: 4881: 4879: 4876: 4875: 4873: 4871: 4866: 4862: 4856: 4853: 4851: 4848: 4846: 4843: 4842: 4840: 4838: 4833: 4829: 4821: 4818: 4817: 4816: 4813: 4811: 4808: 4806: 4803: 4801: 4798: 4794: 4791: 4788: 4785: 4783: 4780: 4779: 4778: 4775: 4773: 4770: 4768: 4765: 4763: 4760: 4758: 4755: 4754: 4752: 4750: 4745: 4741: 4736: 4732: 4725: 4720: 4718: 4713: 4711: 4706: 4705: 4702: 4695: 4691: 4688: 4686: 4683: 4682: 4671: 4667: 4663: 4659: 4655: 4651: 4646: 4642: 4638: 4633: 4628: 4623: 4618: 4614: 4610: 4606: 4601: 4597: 4593: 4588: 4583: 4578: 4573: 4569: 4565: 4561: 4556: 4555: 4540: 4535: 4530: 4525: 4521: 4517: 4513: 4507: 4499: 4495: 4491: 4487: 4483: 4479: 4475: 4471: 4468:(3): 314–21. 4467: 4463: 4456: 4448: 4444: 4440: 4436: 4433:(2): 111–23. 4432: 4428: 4421: 4413: 4409: 4405: 4401: 4397: 4393: 4390:(3): 255–60. 4389: 4385: 4378: 4372: 4371: 4366: 4361: 4353: 4349: 4345: 4341: 4337: 4333: 4326: 4318: 4314: 4309: 4304: 4299: 4294: 4290: 4286: 4282: 4280: 4271: 4263: 4259: 4255: 4251: 4247: 4243: 4240:(1): 133–41. 4239: 4235: 4228: 4220: 4216: 4211: 4206: 4202: 4198: 4193: 4188: 4184: 4180: 4176: 4169: 4161: 4157: 4152: 4147: 4143: 4139: 4135: 4131: 4127: 4120: 4104: 4100: 4096: 4090: 4082: 4078: 4073: 4068: 4064: 4060: 4056: 4052: 4048: 4041: 4033: 4032: 4024: 4016: 4015: 4006: 3998: 3994: 3990: 3986: 3983:(4): 337–41. 3982: 3978: 3971: 3963: 3959: 3955: 3951: 3947: 3943: 3936: 3920: 3916: 3912: 3908: 3904: 3900: 3896: 3892: 3888: 3884: 3877: 3869: 3865: 3861: 3857: 3853: 3849: 3842: 3834: 3830: 3826: 3822: 3818: 3814: 3807: 3791: 3787: 3783: 3779: 3775: 3769: 3761: 3757: 3753: 3749: 3746:(5): 355–62. 3745: 3741: 3733: 3725: 3721: 3717: 3713: 3710:(3): 224–30. 3709: 3705: 3698: 3690: 3686: 3682: 3678: 3673: 3668: 3665:(4): 907–16. 3664: 3660: 3656: 3649: 3641: 3637: 3633: 3629: 3625: 3622:(in French). 3621: 3614: 3606: 3602: 3598: 3594: 3591:(4): 228–36. 3590: 3586: 3579: 3571: 3567: 3562: 3557: 3552: 3547: 3543: 3539: 3535: 3531: 3527: 3520: 3512: 3508: 3503: 3498: 3494: 3490: 3486: 3482: 3478: 3471: 3469: 3449: 3442: 3436: 3417: 3410: 3408: 3399: 3391: 3387: 3382: 3377: 3373: 3369: 3364: 3359: 3355: 3351: 3347: 3340: 3332: 3328: 3323: 3318: 3313: 3308: 3304: 3300: 3297:(6): e99209. 3296: 3292: 3288: 3281: 3273: 3269: 3264: 3259: 3255: 3251: 3247: 3243: 3239: 3232: 3224: 3220: 3216: 3212: 3207: 3202: 3198: 3194: 3190: 3186: 3182: 3178: 3174: 3167: 3159: 3155: 3150: 3145: 3140: 3135: 3131: 3127: 3123: 3116: 3107: 3102: 3097: 3092: 3088: 3084: 3080: 3073: 3065: 3061: 3057: 3053: 3050:(4): 380–91. 3049: 3045: 3038: 3030: 3026: 3021: 3016: 3012: 3008: 3004: 3000: 2996: 2989: 2987: 2978: 2974: 2969: 2964: 2960: 2956: 2952: 2948: 2944: 2937: 2935: 2926: 2922: 2917: 2912: 2908: 2904: 2901:(5): 739–45. 2900: 2896: 2892: 2885: 2877: 2873: 2868: 2863: 2858: 2853: 2849: 2845: 2841: 2834: 2826: 2822: 2817: 2812: 2808: 2804: 2800: 2796: 2792: 2785: 2777: 2773: 2768: 2763: 2759: 2755: 2751: 2747: 2743: 2736: 2728: 2724: 2720: 2716: 2709: 2701: 2697: 2693: 2689: 2685: 2681: 2673: 2665: 2661: 2657: 2653: 2649: 2645: 2641: 2637: 2633: 2626: 2618: 2614: 2609: 2604: 2599: 2594: 2590: 2586: 2582: 2575: 2567: 2563: 2558: 2553: 2549: 2545: 2541: 2537: 2533: 2526: 2510: 2506: 2502: 2496: 2480: 2476: 2472: 2466: 2458: 2454: 2449: 2444: 2440: 2436: 2432: 2428: 2424: 2417: 2415: 2406: 2402: 2397: 2392: 2388: 2384: 2381:(3713): 837. 2380: 2376: 2372: 2365: 2357: 2353: 2349: 2345: 2341: 2337: 2333: 2329: 2325: 2321: 2317: 2310: 2302: 2298: 2294: 2290: 2286: 2282: 2278: 2274: 2267: 2259: 2255: 2251: 2247: 2243: 2239: 2232: 2230: 2221: 2217: 2212: 2207: 2203: 2199: 2195: 2191: 2187: 2180: 2176: 2166: 2163: 2161: 2160: 2155: 2153: 2150: 2149: 2143: 2141: 2138: 2134: 2133: 2128: 2127: 2123:. The suffix 2122: 2121: 2116: 2112: 2108: 2105: 2101: 2100: 2095: 2094: 2089: 2085: 2081: 2071: 2068: 2065: 2061: 2053: 2051: 2047: 2037: 2034: 2032: 2031:cephalosporin 2028: 2018: 2015: 2010: 1999: 1997: 1996: 1988: 1983: 1981: 1977: 1976: 1975:K. pneumoniae 1971: 1967: 1966:ciprofloxacin 1963: 1959: 1955: 1951: 1947: 1943: 1939: 1935: 1931: 1927: 1923: 1919: 1918: 1913: 1912: 1904: 1900: 1890: 1888: 1884: 1880: 1877:Strains with 1870: 1868: 1864: 1860: 1850: 1848: 1844: 1840: 1836: 1832: 1828: 1824: 1820: 1816: 1812: 1802: 1800: 1796: 1792: 1787: 1785: 1781: 1777: 1773: 1769: 1764: 1762: 1758: 1755: 1751: 1736: 1734: 1730: 1726: 1722: 1718: 1714: 1713: 1712:K. pneumoniae 1708: 1704: 1700: 1696: 1692: 1689: 1685: 1681: 1677: 1673: 1669: 1665: 1660: 1656: 1652: 1648: 1644: 1640: 1625: 1622: 1621: 1616: 1615: 1610: 1604: 1594: 1591: 1586: 1578: 1576: 1569:CMY (class C) 1566: 1564: 1560: 1556: 1555: 1549: 1546: 1538: 1537:K. pneumoniae 1532: 1530: 1520: 1516: 1514: 1513:P. aeruginosa 1503: 1501: 1500: 1499:Acinetobacter 1495: 1494: 1482: 1473: 1471: 1470: 1465: 1464: 1460: 1459:Acinetobacter 1456: 1451: 1450: 1446: 1441: 1437: 1433: 1428: 1427: 1422: 1418: 1417: 1412: 1411: 1406: 1405: 1393: 1391: 1387: 1383: 1379: 1375: 1371: 1367: 1363: 1359: 1355: 1351: 1347: 1346: 1341: 1340: 1335: 1334: 1329: 1328: 1327:K. pneumoniae 1323: 1322: 1310: 1308: 1304: 1300: 1296: 1292: 1288: 1284: 1280: 1276: 1272: 1262: 1259: 1258: 1257:P. aeruginosa 1247: 1244: 1243: 1238: 1237: 1236:P. aeruginosa 1232: 1228: 1227: 1226:K. pneumoniae 1222: 1221: 1216: 1212: 1208: 1204: 1200: 1195: 1185: 1183: 1182: 1177: 1173: 1172:K. pneumoniae 1169: 1165: 1161: 1157: 1152: 1151: 1146: 1142: 1138: 1134: 1124: 1121: 1120: 1119:K. pneumoniae 1109: 1106: 1102: 1101: 1100:K. pneumoniae 1096: 1095: 1090: 1089: 1084: 1083: 1082:H. influenzae 1078: 1077: 1072: 1057: 1055: 1051: 1047: 1042: 1038: 1034: 1030: 1026: 1015: 1013: 1009: 1005: 1001: 997: 993: 989: 985: 981: 977: 973: 969: 965: 961: 957: 953: 949: 948: 943: 942: 937: 936: 935:K. pneumoniae 931: 930: 929:P. aeruginosa 925: 924: 923:S. marcescens 919: 918: 913: 912: 900: 897: 889: 879: 874: 870: 866: 865: 858: 849: 848: 840: 838: 834: 830: 825: 823: 819: 815: 808:Penicillinase 805: 801: 797: 789: 787: 783: 779: 773: 767: 760: 759: 754: 750: 746: 745: 734: 732: 727: 725: 721: 717: 713: 709: 705: 701: 697: 693: 689: 685: 682:that provide 681: 677: 674: 670: 666: 662: 655: 651: 650: 645: 638: 634: 630: 625: 613: 610: 608: 604: 601: 598: 596: 592: 589: 586: 584: 580: 575: 571: 568: 564: 561: 559: 558:Gene Ontology 555: 552: 549: 546: 543: 540: 536: 533: 530: 528: 524: 521: 518: 516: 512: 509: 506: 504: 500: 497: 496:NiceZyme view 494: 492: 488: 485: 482: 480: 476: 473: 470: 468: 464: 459: 456: 453: 451: 447: 444: 441: 439: 435: 430: 425: 419: 414: 409: 398: 395: 393: 389: 386: 382: 378: 375: 373: 369: 365: 361: 358: 355: 351: 346: 342: 339: 336: 334: 330: 327: 324: 321: 317: 314: 311: 309: 305: 301: 297: 292: 285: 280: 275: 262: 256: 250: 244: 238: 232: 226: 220: 214: 208: 202: 196: 192: 190: 186: 183: 180: 178: 174: 171: 167: 163: 160: 158: 154: 150: 146: 143: 140: 136: 131: 127: 124: 120: 116: 113: 111: 107: 104: 101: 99: 95: 92: 89: 87: 83: 80: 77: 74: 70: 67: 64: 62: 58: 54: 50: 45: 40: 39: 35:Structure of 32: 27: 22: 19: 5285:Translocases 5282: 5269: 5256: 5243: 5230: 5220:Transferases 5217: 5204: 5061:Binding site 4849: 4777:Aminoacylase 4757:Asparaginase 4653: 4649: 4615:(1): 29–57. 4612: 4608: 4567: 4563: 4519: 4515: 4506: 4465: 4461: 4455: 4430: 4426: 4420: 4387: 4383: 4377: 4368: 4360: 4335: 4331: 4325: 4288: 4284: 4278: 4270: 4237: 4233: 4227: 4182: 4178: 4168: 4136:(4): 283–8. 4133: 4129: 4119: 4107:. Retrieved 4098: 4089: 4057:(2): 100–6. 4054: 4050: 4040: 4030: 4023: 4012: 4005: 3980: 3976: 3970: 3945: 3941: 3935: 3923:. Retrieved 3890: 3886: 3876: 3854:(2): 181–7. 3851: 3847: 3841: 3819:(6): 593–4. 3816: 3812: 3806: 3794:. Retrieved 3777: 3768: 3743: 3739: 3732: 3707: 3703: 3697: 3662: 3658: 3648: 3626:(1): 39–45. 3623: 3619: 3613: 3588: 3584: 3578: 3533: 3529: 3519: 3484: 3480: 3455:. Retrieved 3435: 3423:. Retrieved 3416:the original 3406: 3398: 3353: 3349: 3339: 3294: 3290: 3280: 3245: 3241: 3231: 3180: 3176: 3166: 3129: 3125: 3115: 3086: 3082: 3072: 3047: 3043: 3037: 3002: 2998: 2950: 2946: 2898: 2894: 2884: 2867:10400.18/206 2847: 2843: 2833: 2798: 2794: 2784: 2749: 2745: 2735: 2718: 2714: 2708: 2683: 2679: 2672: 2639: 2635: 2625: 2588: 2584: 2574: 2539: 2535: 2525: 2513:. Retrieved 2504: 2495: 2483:. Retrieved 2474: 2465: 2430: 2426: 2378: 2374: 2364: 2323: 2319: 2309: 2276: 2272: 2266: 2241: 2237: 2196:(6): 783–6. 2193: 2189: 2179: 2158: 2139: 2130: 2124: 2118: 2110: 2106: 2097: 2091: 2077: 2069: 2062:, which are 2054: 2043: 2035: 2024: 2005: 1993: 1991: 1986: 1973: 1949: 1915: 1909: 1907: 1902: 1898: 1878: 1876: 1856: 1827:Co-amoxiclav 1808: 1794: 1790: 1788: 1775: 1771: 1767: 1765: 1756: 1747: 1728: 1720: 1710: 1706: 1690: 1668:trimethoprim 1658: 1638: 1636: 1618: 1612: 1606: 1589: 1587: 1584: 1574: 1572: 1552: 1550: 1542: 1536: 1528: 1526: 1517: 1512: 1509: 1497: 1491: 1488: 1479: 1469:Enterobacter 1467: 1453: 1443: 1424: 1416:Enterobacter 1414: 1408: 1402: 1399: 1378:co-ticarclav 1366:co-amoxiclav 1343: 1339:P. mirabilis 1337: 1331: 1325: 1319: 1316: 1283:sulfonamides 1268: 1255: 1253: 1240: 1234: 1229:, and other 1224: 1218: 1191: 1179: 1175: 1171: 1167: 1148: 1130: 1117: 1115: 1098: 1092: 1086: 1080: 1075: 1068: 1021: 947:P. mirabilis 945: 939: 933: 927: 921: 915: 909: 907: 892: 883: 876:Please help 872: 861: 828: 826: 811: 802: 798: 795: 780:is given by 774: 756: 744:Streptomyces 742: 740: 728: 665:β-lactamases 664: 660: 659: 653: 647: 639:ring in red. 484:BRENDA entry 36: 18: 5056:Active site 4965:: Nitriles/ 4845:Barbiturase 4772:Biotinidase 4762:Glutaminase 4109:24 December 3925:24 December 3796:24 December 3457:14 November 3425:19 November 3183:(1): 4224. 2515:11 February 2485:11 February 2433:(1): 1–11. 2115:lactic acid 1946:ceftazidime 1938:Ceftriaxone 1867:carbapenems 1863:cephamycins 1835:clavulanate 1831:ticarcillin 1823:clavulanate 1819:amoxicillin 1754:carbapenems 1750:cephamycins 1725:carbapenems 1695:Cephamycins 1680:clavulanate 1643:cephamycins 1590:B. fragilis 1493:Pseudomonas 1463:Citrobacter 1449:Pseudomonas 1404:Citrobacter 1374:clavulanate 1370:ticarcillin 1362:clavulanate 1358:amoxicillin 1211:cloxacillin 1203:cephalothin 1156:ceftazidime 1141:ceftriaxone 1137:ceftazidime 1046:Carbapenems 1033:ceftazidime 1029:ceftriaxone 1004:cephamycins 996:carbapenems 984:clavulanate 972:cephamycins 964:ceftazidime 960:ceftriaxone 952:ceftizoxime 917:C. freundii 880:if you can. 833:methicillin 818:hydrolysing 816:, again by 814:penicillins 720:beta-lactam 716:antibiotics 708:carbapenems 704:monobactams 700:cephamycins 692:penicillins 637:Beta-lactam 629:penicillins 472:IntEnz view 432:Identifiers 411:β-lactamase 294:Identifiers 47:Identifiers 5328:Categories 5259:Isomerases 5233:Hydrolases 5100:Regulation 4883:Agmatinase 4800:Ceramidase 4731:Hydrolases 3893:(4): 658. 3887:Pediatrics 3089:(4): 709. 2244:: 96–105. 2171:References 2165:Nitrocefin 2135:(from the 2102:(from the 2027:nitrocefin 1954:cephamycin 1942:cefotaxime 1917:Klebsiella 1903:Klebsiella 1843:tazobactam 1793:–type and 1688:tazobactam 1548:plasmids. 1545:amino acid 1438:, whereas 1436:tazobactam 1386:tazobactam 1307:gentamicin 1295:mecillinam 1291:fosfomycin 1279:quinolones 1199:ampicillin 1160:cefotaxime 1133:cefotaxime 1025:cefotaxime 1006:) such as 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