1035:. In both plant and mammalian enzymes, the N-terminal domain contains an eight-stranded antiparallel β-barrel, but in the soybean lipoxygenases this domain is significantly larger than in the rabbit enzyme. The plant lipoxygenases can be enzymatically cleaved into two fragments which stay tightly associated while the enzyme remains active; separation of the two domains leads to loss of catalytic activity. The C-terminal (catalytic) domain consists of 18-22 helices and one (in rabbit enzyme) or two (in soybean enzymes) antiparallel β-sheets at the opposite end from the N-terminal β-barrel.
951:(also termed leukocyte-type 12-Lox, 12-Lox-l, and 12/15-Lox) differs from human ALOX15, which under standard assay conditions metabolizes arachidonic acid to 15-HpETE and 12-HpETE products in an 89 to 11 ratio, metabolizes arachidonic acid to 15-Hpete and 12-HpETE in a 1 to 6 ratio, i.e. its principal metabolite is 12-HpETE. Also, human ALOX15 prefers linoleic acid over arachidonic acid as a substrate, metabolizing it to 13-HpODE while Alox15 has little or no activity on linoleic acid. Alox15 can metabolize polyunsaturated fatty acids that are esterified to
1055:(His) ligands to the active site iron. Two cavities in the major domain of soybean lipoxygenase-1 (cavities I and II) extend from the surface to the active site. The funnel-shaped cavity I may function as a dioxygen channel; the long narrow cavity II is presumably a substrate pocket. The more compact mammalian enzyme contains only one boot-shaped cavity (cavity II). In soybean lipoxygenase-3 there is a third cavity which runs from the iron site to the interface of the
3152:
500:
1010:
33:
826:), also termed eLOX3 and lipoxygenase, epidermis type. Unlike other lipoxygenases, ALOXE3 exhibits only a latent dioxygenase activity. Rather, its primary activity is as a hydroperoxide isomerase that metabolizes certain unsaturated hydroperoxy fatty acids to their corresponding epoxy alcohol and epoxy keto derivatives and thereby is also classified as a
415:. Certain types of the lipoxygenases, e.g. human and murine 15-lipoxygenase 1, 12-lipoxygenase B, and ALOXE3, are capable of metabolizing fatty acid substrates that are constituents of phospholipids, cholesterol esters, or complex lipids of the skin. Most lipoxygenases catalyze the formation of initially formed hydroperoxy products that have
1293:(KIE) on kcat (kH/kD) (81 near room temperature) so far reported for a biological system. Recently, an extremely elevated KIE of 540 to 730 was found in a double mutant Soybean Lipoxygenase 1. Because of the large magnitude of the KIE, Soybean Lipoxygenase 1 has served as the prototype for enzyme-catalyzed hydrogen-tunneling reactions.
1074:
Details about the active site feature of lipoxygenase were revealed in the structure of porcine leukocyte 12-lipoxygenase catalytic domain complex In the 3D structure, the substrate analog inhibitor occupied a U-shaped channel open adjacent to the iron site. This channel could accommodate arachidonic
1043:
The iron atom in lipoxygenases is bound by four ligands, three of which are histidine residues. Six histidines are conserved in all lipoxygenase sequences, five of them are found clustered in a stretch of 40 amino acids. This region contains two of the three zinc-ligands; the other histidines have
976:
Alox12e (12-Lox-e, epidermal-type 12-Lox) is an ortholog to the human ALOX12P gene which has suffered damaging mutations and is not expressed. ALox12e prefers methyl esters over non-esterified polyunsaturated fatty acid substrates, metabolizing linoleic acid ester to its 13-hydroperoxy counterpart
429:
and diacylglycerol lipases are activated during cell stimulation, proceed to release these fatty acids from their storage sites, and thereby are key regulators in the formation of lipoxygenase-dependent metabolites. In addition, cells, when so activated, may transfer their released polyunsaturated
272:
The lipoxygenases are related to each other based upon their similar genetic structure and dioxygenation activity. However, one lipoxygenase, ALOXE3, while having a lipoxygenase genetic structure, possesses relatively little dioxygenation activity; rather its primary activity appears to be as an
927:
The mouse is a common model to examine lipoxygenase function. However, there are some key differences between the lipoxygenases between mice and men that make extrapolations from mice studies to humans difficult. In contrast to the 6 functional lipoxygenases in humans, mice have 7 functional
894:
Two lipoxygenases may act in series to make di-hydroxy or tri-hydroxy products that have activities quite different than either lipoxyenases' products. This serial metabolism may occur in different cell types that express only one of the two lipoxygenases in a process termed transcellular
932:. In particular, mouse Alox15, unlike human ALOX15, metabolizes arachidonic acid mainly to 12-HpETE and mouse Alox15b, in contrast to human ALOX15b, is primarily an 8-lipoxygenase, metabolizing arachdionic acid to 8-HpETE; there is no comparable 8-HpETE-forming lipoxygenase in humans.
1075:
acid without much computation, defining the substrate binding details for the lipoxygenase reaction. In addition, a plausible access channel, which intercepts the substrate binding channel and extended to the protein surface could be counted for the oxygen path.
987:-hydroperoxy counterpart and thereby contribute to skin integrity and water impermeability; mice depleted to Alox12b develop a severe skin defect similar to Congenital ichthyosiform erythroderma. Unlike human ALOX12B which cam metabolize arachidonic acid to 12
1022:
There are several lipoxygenase structures known including: soybean lipoxygenase L1 and L3, coral 8-lipoxygenase, human 5-lipoxygenase, rabbit 15-lipoxygenase and porcine leukocyte 12-lipoxygenase catalytic domain. The protein consists of a small N-terminal
1070:
is weakly associated with the iron. In rabbit lipoxygenase, this Asn residue is replaced with His which coordinates the iron via N atom. Thus, the coordination number of iron is either five or six, with a hydroxyl or water ligand to a hexacoordinate iron.
721:), also termed 15-lipoxygenase-1, erythrocyte type 15-lipoxygenase (or 15-lipoxygenase, erythrocyte type), reticulocyte type 15-lipoxygenase (or 15-lipoxygenase, reticulocyte type), 15-LO-1, and 15-LOX-1. It metabolizes arachidonic acid principally to
438:
These enzymes are most common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. In mammals a number of lipoxygenases
969:(also termed 8-lipoxygenase, 8-lox, and 15-lipoxygenase type II), in contrast to ALOX15B which metabolizes arachidonic acid principally to 15-HpETE and to a lesser extent linoleic acid to 13-HpODE, metabolizes arachidonic acid principally to 8
642:
to a set of metabolites that contain 5 double bounds (i.e. 5-HEPE, 5-oxo-EPE, LTB5, LTC5, LTD5, and LTE5) as opposed to the 4 double bond-containing arachidonic acid metabolites. The enzyme, when acting in series with other lipoxygenase,
686:), also termed 12-lipoxygenase, platelet type platelet lipoxygenase (or 12-lipoxygenase, platelet type) 12-LOX, and 12-LO. It metabolizes arachidonic acid to 12-hydroperoxyeiocsatetraeoic acid (12-HpETE) which is further metabolized to
1005:-hydoperoxy-linoleate derivative of EOS to its epoxy and keto derivatives and to be involved in maintaining skin integrity and water impermeability. AloxE3 deletion leads to a defect similar to congenital ichthyosiform erythroderma.
881:
EOS analogs. ALOXE3 is thought to act with ALOX12B in skin epidermis to form the latter two EOS analogs; inactivation mutations of ALOX3 are, similar to inactivating mutations in ALOX12B, associated with autosomal recessive
2810:
776:. ALOX15B has little or no ability to metabolize arachidonic acid to 12-hydroperoxeiocosatetraenoic acid (12-(HpETE) and only minimal ability to metabolize linoleic acid to 13-hydroperoxyoctadecaenoic acid (13-HpODE).
963:). This property along with its dual specificity in metabolizing arachidonic acid to 12-HpETE and 15-HpETE are similar to those of human ALOX15 and has led to both enzymes being termed 12/15-lipoxygenases.
765:. This property along with its dual specificity in metabolizing arachidonic acid to 12-HpETE and 15-HpETE are similar to those of mouse Alox15 and has led to both enzymes being termed 12/15-lipoxygenases.
1880:
945:
differs from human ALOX12, which preferentially metabolizes arachidonic acid to 12-HpETE but also to substantial amounts of 15-HpETE, in that metabolizes arachidonic acid almost exclusively to 12-HpETE.
308:), and a relatively large C-terminal catalytic domain which contains the non-heme iron critical for the enzymes' catalytic activity. Most of the lipoxygenases (exception, ALOXE3) catalyze the reaction
564:
boundaries at highly conserved positions. The 6 human lipoxygenases along with some of the major products that they make, as well as some of their associations with genetic diseases, are as follows:
288:, possesses proteins with a slight (~20%) amino acid sequence similarity to lipoxygenases, these proteins lack iron-binding residues and therefore are not projected to possess lipoxygenase activity.
425:
Lipoxygenases depend on the availability of their polyunsaturated fatty acid substrates which, particularly in mammalian cells, is normally maintained at extremely low levels. In general, various
811:
end and esterified to linoleic acid at its omega hydroxyl end. In skin epidermal cells, ALOX12B metabolizes the linoleate in this esterified omega-hydroxyacyl-sphingosine (EOS) to its 9
2441:
430:
fatty acids to adjacent or nearby cells which then metabolize them through their lipoxygenase pathways in a process termed transcellular metabolism or transcellular biosynthesis.
772:), also termed 15-lipoxygenase-2, 15-LOX-2, and 15-LOX-2. It metabolizes arachidonic acid to 15-hydroperoxyeicosatetraenoic (15-HpETE) which is further metabolized to
168:
2281:
Steczko J, Donoho GP, Clemens JC, Dixon JE, Axelrod B (1992). "Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement".
1397:"Biosynthesis, biological effects, and receptors of hydroxyeicosatetraenoic acids (HETEs) and oxoeicosatetraenoic acids (oxo-ETEs) derived from arachidonic acid"
1062:
The active site iron is coordinated by N of three conserved His residues and one oxygen of the C-terminal carboxyl group. In addition, in soybean enzymes the
1352:
Choi J, Chon JK, Kim S, Shin W (February 2008). "Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data".
2722:
2579:
2527:
124:
112:
799:-hydroxyeicosatetraenoic acid but does so only with low catalytic activity; its most physiologically important substrate is thought to be a
991:-HETE at a low rate, Alox12b does not metabolize arachidonic acid as free acid but dose metabolize arachidonic acid methyl ester to its 12
2367:"Extremely elevated room-temperature kinetic isotope effects quantify the critical role of barrier width in enzymatic C-H activation"
900:
895:
metabolism. For example, ALOX5 and ALOX15 or, alternatively, ALOX5 and ALOX12 can act serially to metabolize arachidonic acid into
2696:
1603:
Capra V, Rovati GE, Mangano P, Buccellati C, Murphy RC, Sala A (2015). "Transcellular biosynthesis of eicosanoid lipid mediators".
344:
The (—OO) residue may then be protonated to form a hydroperoxide group (—OOH) and further metabolized by the lipoxygenase to e.g.
745:
over arachidonic acid, metabolizing linoleic acid to 12-hydroperoxyoctadecaenoic acid (13-HpODE) which is further metabolized to
2450:
2829:
2318:"Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis"
1708:"A novel lipoxygenase from rice. Primary structure and specific expression upon incompatible infection with rice blast fungus"
3201:
1844:
Haeggström, J. Z.; Funk, C. D. (2011). "Lipoxygenase and leukotriene pathways: Biochemistry, biology, and roles in disease".
883:
816:
92:
1969:
Romano M, Cianci E, Simiele F, Recchiuti A (2015). "Lipoxins and aspirin-triggered lipoxins in resolution of inflammation".
904:
188:
2365:
Hu, S; Sharma, S. C.; Scouras, A. D.; Soudackov, A. V.; Carr, C. A.; Hammes-Schiffer, S; Alber, T; Klinman, J. P. (2014).
1059:
and catalytic domains. Cavity III, the iron site and cavity II form a continuous passage throughout the protein molecule.
983:(e-LOX2, epidermis-type Lox-12) appears to act similarly to ALOX12B to metabolize the linoleic acid moiety of EOS to its 9
284:
Lipoxygenases are found in eukaryotes (plants, fungi, animals, protists); while the third domain of terrestrial life, the
2790:
2572:
2141:
Taylor, P. R.; Heydeck, D; Jones, G. W.; Krönke, G; Funk, C. D.; Knapper, S; Adams, D; Kühn, H; O'Donnell, V. B. (2012).
631:
353:
815:-hydroperoxy analog. Inactivating mutations of ALOX12B are associated with the human skin disease, autosomal recessive
296:
Based on detailed analyses of 15-lipoxygenase 1 and stabilized 5-lipoxygenase, lipoxygenase structures consist of a 15
2871:
2238:
Boyington JC, Gaffney BJ, Amzel LM (1993). "The three-dimensional structure of an arachidonic acid 15-lipoxygenase".
1655:
734:
695:
687:
886:
in humans. Inactivating mutations in ALOX3 are also associated with the human disease lamellar ichthyosis (see
2565:
973:-HpETE and linoleic acid to 9-HpODE. Alox15b is as effective as ALOX5 in metabolizing 5-HpETE to leukotrienes.
773:
746:
726:
701:
305:
176:
3027:
2780:
1638:
Vick BA, Zimmerman DC (1987). "Oxidative
Systems for Modification of Fatty Acids: The Lipoxygenase Pathway".
596:
2756:
2742:
2689:
2557:
1174:
1129:
803:
which contains a very long chain (16-34 carbons) omega-hydroxyl fatty acid that is in amide linkage to the
666:
361:
2795:
2751:
2737:
1251:
1219:
600:
568:
3142:
493:
172:
503:
An illustrative transformation involving a hydroperoxide lyase. Here cis-3-hexenal is generated from
384:
371:
Polyunsaturated fatty acids that serve as substrates for one or more of the lipoxygenases include the
3128:
3115:
3102:
3089:
3076:
3063:
3050:
3012:
2765:
105:
337:) to the rearranged carbon radical center thereby forming a peroxy radical(—OO·) bond to that carbon
3022:
2976:
2919:
2713:
2542:
1671:
Needleman P, Turk J, Jakschik BA, Morrison AR, Lefkowith JB (1986). "Arachidonic acid metabolism".
1243:
1211:
1166:
1121:
1086:
705:
670:
572:
468:
422:. Exceptions to this rule include the 12R-lipoxygenases of humans and other mammals (see below).
204:
1047:
The two long central helices cross at the active site; both helices include internal stretches of
2924:
2682:
2653:
2524: – structure of the catalytic domain of porcine leukocyte 12-lipoxygenasean with inhibitor
1747:
KenjiMatsui (2006). "Green leaf volatiles: hydroperoxide lyase pathway of oxylipin metabolism".
1290:
916:
360:
to a hydroxy group thereby forming hydroxylated (—OH) polyunsaturated fatty acids such as the
2945:
2864:
2596:
912:
639:
484:) as well as what seems to be a chloroplast isozyme. Plant lipoxygenase in conjunction with
456:
396:
365:
2674:
2548:
273:
isomerase that catalyzes the conversion of hydroperoxy unsaturated fatty acids to their 1,5-
3196:
3017:
2785:
2775:
2663:
2247:
1926:
Qu Q, Xuan W, Fan GH (2015). "Roles of resolvins in the resolution of acute inflammation".
1756:
656:
651:
enzymes, contributes to the metabolism of eicosapentaenoic acid to E series resolvins (see
404:
400:
324:
155:
928:
lipoxygenases and some of the latter have different metabolic activities than their human
8:
3186:
2981:
2552:
2203:
2066:"The importance of the lipoxygenase-hepoxilin pathway in the mammalian epidermal barrier"
485:
2538:
2531:
2414:
2251:
1760:
1684:
2914:
2838:
2800:
2648:
2391:
2366:
2342:
2317:
2212:
2191:
2167:
2142:
2090:
2065:
1951:
1908:
1647:
1580:
1555:
1531:
1506:
1479:
1454:
1421:
1396:
1377:
960:
758:
408:
392:
372:
1724:
1707:
1001:(epidermis-type Lox-3, eLox3) appears to act similarly to ALOXe3 in metabolizing the 9
117:
2516:
2504:
2480:
2464:
2447:
2396:
2347:
2298:
2263:
2217:
2172:
2095:
1986:
1943:
1900:
1861:
1812:
1772:
1729:
1688:
1651:
1620:
1585:
1536:
1484:
1426:
1369:
227:
163:
97:
1955:
1912:
1556:"The role of lipoxygenases in pathophysiology; new insights and future perspectives"
1381:
749:(13-HODE). ALOX15 can metabolize polyunsaturated fatty acids that are esterified to
524:
genes are located on chromosome 17.p13 and code for a single chain protein of 75–81
488:
are responsible for many fragrances and other signalling compounds. One example is
61:
3191:
2960:
2955:
2929:
2857:
2615:
2386:
2378:
2337:
2329:
2290:
2255:
2207:
2199:
2162:
2154:
2085:
2077:
1978:
1935:
1892:
1853:
1804:
1764:
1719:
1680:
1643:
1612:
1575:
1567:
1526:
1518:
1474:
1466:
1416:
1408:
1361:
589:
426:
376:
151:
2549:
Blanch Time and
Cultivar Effects on Quality of Frozen and Stored Corn and Broccoli
129:
3172:
3007:
2991:
2904:
2588:
2454:
2158:
2081:
1982:
1896:
1808:
1616:
1470:
1412:
717:
682:
648:
584:
480:
239:
73:
2116:
1831:"ALOX5 arachidonate 5-lipoxygenase [Homo sapiens (human)] - Gene - NCBI"
1571:
977:
and to a lesser extent arachidonic acid ester to its 12-hydroperoxy counterpart.
588:), also termed 5-lipoxygenase, 5-LOX, and 5-LO. Major products: it metabolizes
3156:
3045:
2986:
2705:
2592:
1640:
Oxidative systems for the modification of fatty acids: The
Lipoxygenase Pathway
733:
12-hydroperoxyeicosatetraenoic acid (12-HpETE) which is further metabolized to
660:
652:
644:
623:
619:
615:
611:
607:
504:
254:
2333:
2064:
Muñoz-Garcia, A; Thomas, C. P.; Keeney, D. S.; Zheng, Y; Brash, A. R. (2014).
2032:
2004:
1768:
1013:
Rabbit 15-lipoxygenase (blue) with inhibitor (yellow) bound in the active site
725:
15-hydroperoxyeiocatetraenoic acid (15-HpETE) which is further metabolized to
663:). These resolvins are also classified as specialized pro-resolving mediators.
3180:
2950:
2909:
1795:
Krieg, P; FĂĽrstenberger, G (2014). "The role of lipoxygenases in epidermis".
887:
742:
489:
448:
380:
315:
235:
17:
2587:
2259:
2143:"Development of myeloproliferative disease in 12/15-lipoxygenase deficiency"
2899:
2400:
2351:
2221:
2176:
2099:
1990:
1947:
1904:
1881:"n-3 Fatty acid supplementation and proresolving mediators of inflammation"
1865:
1816:
1776:
1624:
1589:
1540:
1488:
1430:
1373:
952:
908:
842:
750:
507:
to the hydroperoxide by the action of a lipoxygenase followed by the lyase.
388:
2302:
2267:
2070:
Biochimica et
Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
1797:
Biochimica et
Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
1733:
1692:
1605:
Biochimica et
Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
1522:
1459:
Biochimica et
Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
1401:
Biochimica et
Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
1246:
1214:
1169:
1124:
1089:
708:
673:
575:
471:
101:
3123:
3058:
2894:
2643:
2627:
2622:
1056:
1032:
1024:
956:
800:
762:
754:
525:
452:
345:
301:
207:
2294:
1830:
907:
of 15(S)-HpETE, 15(S)-HETE, 15(R)-HpETE, 15(R)-HETE, and 15-oxo-ETE and
2819:
2512: – structure of rabbit 15-lipoxygenase in complex with inhibitor
1939:
1507:"Advances in Our Understanding of Oxylipins Derived from Dietary PUFAs"
1365:
1333:
1067:
1063:
444:
357:
297:
250:
242:
85:
2520:
2508:
2484:
2468:
2382:
1857:
1345:
3097:
3071:
2709:
1052:
911:) while ALOX15 and possibly ALOX15B can act with ALOX5 to metabolize
827:
738:
691:
592:
to 5-hydroperoxy-eicostetraeoic acid (5-HpETE) which is converted to
419:
412:
349:
266:
262:
258:
1009:
3168:
3151:
2610:
1325:
1048:
929:
849:
hydroperoxy unsaturated fatty acids and efficiently converts the 9(
712:
677:
579:
475:
278:
231:
68:
2551:– lipoxygenase, peroxidase, cystine lyase enzyme inactivation in
2315:
1706:
Tanaka K, Ohta H, Peng YL, Shirano Y, Hibino T, Shibata D (1994).
499:
2458:
2059:
2057:
2055:
2053:
1309:
1301:
980:
966:
896:
808:
780:
769:
635:
440:
323:
the rate-limiting step of hydrogen abstraction from a bisallylic
285:
274:
80:
2488: – structure of soybean lipoxygenase-3 in complex with (9
2190:
Cole, B. K.; Lieb, D. C.; Dobrian, A. D.; Nadler, J. L. (2013).
340:
reduction of the peroxy radical to its corresponding anion (—OO)
304:
domain, a small (e.g. ~0.6 kilodalton) linker inter-domain (see
3110:
2880:
2760:
2746:
1505:
Gabbs M, Leng S, Devassy JG, Monirujjaman M, Aukema HM (2015).
1317:
1305:
1297:
998:
948:
942:
823:
561:
459:). Sequence data is available for the following lipoxygenases:
223:
183:
2050:
1296:
Human proteins expressed from the lipoxygenase family include
1044:
been shown to be important for the activity of lipoxygenases.
3084:
2704:
2063:
1670:
1313:
936:
246:
1968:
1790:
1788:
1786:
1602:
1504:
1336:; consequently, ALOX12P2 protein is not detected in humans.
3164:
1028:
557:
219:
215:
145:
56:
2849:
261:
signals that regulate the function of their parent cells,
2280:
2192:"12- and 15-lipoxygenases in adipose tissue inflammation"
1783:
520:), which is located on chromosome 10q11.2, all six human
433:
2364:
2140:
1455:"Mammalian lipoxygenases and their biological relevance"
265:
signals that regulate the function of nearby cells, and
32:
3163:
This article incorporates text from the public domain
3140:
2316:
Xu, S.; Mueser T.C.; Marnett L.J.; Funk M.O. (2012).
2237:
2189:
1705:
1452:
467:
Plants express a variety of cytosolic lipoxygenases (
330:
rearrangement of the radical to another carbon center
306:
Protein domain § Domains and protein flexibility
269:
signals that regulate the function of distant cells.
2472: – structure of lipoxygenase-1 from soybean (
853:)-hydroperoxy analog of EOS made by ALOX15B to its 9
845:
of hepoxilins A3 and B3, ALOXE3 favors metabolizing
1794:
327:carbon to form a fatty acid radical at that carbon
37:Structure of rabbit reticulocyte 15S-lipoxygenase.
939:appears to be similar in function to human ALOX5.
3178:
2027:
2025:
1289:Soybean Lipoxygenase 1 exhibits the largest H/D
528:that consists of 662–711 amino acids. Mammalian
356:, or reduced by ubiquitous cellular glutathione
1351:
516:With the exception of the gene encoding 5-LOX (
2233:
2231:
1843:
1553:
1500:
1498:
1448:
1446:
1444:
1442:
1440:
2865:
2690:
2573:
2111:
2109:
2022:
1878:
1637:
1078:
1027:and a major C-terminal catalytic domain (see
899:(see 15-Hydroxyeicosatetraenoic acid §§
729:(15-HETE) but also to far smaller amounts of
1962:
1919:
1872:
1394:
1206:)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
1161:)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
2274:
2228:
1746:
1596:
1547:
1495:
1437:
1388:
1283:)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
917:Resolvin § Biochemistry and production
795:-LO. It metabolizes arachidonic acid to 12
618:(LTC4) (LTC4 may be further metabolized to
2872:
2858:
2697:
2683:
2580:
2566:
2528:UMich Orientation of Proteins in Membranes
2500:)-13-hydroperoxyoctadeca-9,11-dienoic acid
2196:Prostaglandins & Other Lipid Mediators
2106:
1699:
1664:
1631:
2541:at the U.S. National Library of Medicine
2390:
2341:
2211:
2166:
2089:
1925:
1723:
1579:
1530:
1478:
1420:
2371:Journal of the American Chemical Society
1453:Kuhn H, Banthiya S, van Leyen K (2015).
1008:
779:Arachidonate 12-lipoxygenase, 12R type (
498:
1179:(arachidonate:oxygen 15-oxidoreductase)
1134:(arachidonate:oxygen 12-oxidoreductase)
1116:)-13-hydroperoxyoctadeca-9,11-dienoate
3179:
2415:"WikiGenes - Collaborative Publishing"
2117:"WikiGenes - Collaborative Publishing"
2033:"WikiGenes - Collaborative Publishing"
2005:"WikiGenes - Collaborative Publishing"
1256:(arachidonate:oxygen 8-oxidoreductase)
1224:(arachidonate:oxygen 5-oxidoreductase)
922:
768:Arachidonate 15-lipoxygenase type II (
610:(LTA4) which may then be converted to
511:
462:
434:Biological function and classification
2853:
2678:
2561:
884:congenital ichthyosiform erythroderma
834:-hydroperoxyeicosatetraenoic acid (12
830:synthase. While it can metabolize 12
817:congenital ichthyosiform erythroderma
630:acting in series with ALOX15, to the
2419:WikiGenes - Collaborative Publishing
2204:10.1016/j.prostaglandins.2012.07.004
2121:WikiGenes - Collaborative Publishing
2037:WikiGenes - Collaborative Publishing
2009:WikiGenes - Collaborative Publishing
1097:(linoleate:oxygen 13-oxidoreductase)
2791:4-Hydroxyphenylpyruvate dioxygenase
2153:(25): 6173–4, author reply 6174–5.
1685:10.1146/annurev.bi.55.070186.000441
632:specialized pro-resolving mediators
368:(i.e. hydroxyoctadecaenoic acids).
354:specialized pro-resolving mediators
257:agents that serve diverse roles as
13:
1879:Barden AE, Mas E, Mori TA (2016).
1648:10.1016/b978-0-12-675409-4.50009-5
1332:gene in mice, the human gene is a
638:A4 and B4. ALOX5 also metabolizes
443:are involved in the metabolism of
14:
3213:
2448:Lipoxygenases iron-binding region
2435:
1320:. While humans also possess the
3150:
1971:European Journal of Pharmacology
1749:Current Opinion in Plant Biology
31:
2407:
2358:
2309:
2183:
2134:
1997:
1837:
1823:
1740:
1642:. Vol. 9. pp. 53–90.
1017:
807:nitrogen of sphingosine at its
735:12-hydroxyeicosatetraenoic acid
696:12-hydroxyeicosatetraenoic acid
688:12-hydroxyeicosatetraenoic acid
333:addition of molecular oxygen (O
291:
1038:
1031:database), which contains the
774:15-hydroxyicosatetraenoic acid
747:13-hydroxyoctadecadienoic acid
727:15-hydroxyicosatetraenoic acid
702:Arachidonate 15-lipoxygenase-1
310:Polyunsaturated fatty acid + O
1:
2781:Homogentisate 1,2-dioxygenase
1885:Current Opinion in Lipidology
1725:10.1016/S0021-9258(17)41924-7
1554:Mashima R, Okuyama T (2015).
1339:
822:Epidermis-type lipoxygenase (
597:5-hydroxyicosatetraenoic acid
362:hydroxyeicosatetraenoic acids
140:Available protein structures:
3202:Peripheral membrane proteins
2757:Arachidonate 15-lipoxygenase
2743:Arachidonate 12-lipoxygenase
2159:10.1182/blood-2012-02-410928
2082:10.1016/j.bbalip.2013.08.020
1983:10.1016/j.ejphar.2015.03.083
1897:10.1097/MOL.0000000000000262
1809:10.1016/j.bbalip.2013.08.005
1617:10.1016/j.bbalip.2014.09.002
1471:10.1016/j.bbalip.2014.10.002
1413:10.1016/j.bbalip.2014.10.008
1395:Powell WS, Rokach J (2015).
1175:arachidonate 15-lipoxygenase
1130:arachidonate 12-lipoxygenase
667:Arachidonate 12-lipoxygenase
7:
2879:
2796:Indoleamine 2,3-dioxygenase
2752:Arachidonate 8-lipoxygenase
2738:Arachidonate 5-lipoxygenase
1572:10.1016/j.redox.2015.08.006
1252:arachidonate 8-lipoxygenase
1220:arachidonate 5-lipoxygenase
741:. ALOX15 actually prefers
661:Resolvin § Resolvin Ds
659:to D series resolvins (see
653:Resolvin § Resolvin Es
601:5-oxo-eicosatetraenoic acid
569:Arachidonate 5-lipoxygenase
10:
3218:
3162:
1928:Cell Biology International
1079:Biochemical classification
15:
3036:
3028:Michaelis–Menten kinetics
3000:
2969:
2938:
2887:
2828:
2809:
2766:Linoleate 11-lipoxygenase
2721:
2636:
2603:
2334:10.1016/j.str.2012.06.003
1769:10.1016/j.pbi.2006.03.002
995:-hydroperoxy counterpart.
494:odor of freshly cut grass
249:containing a cis,cis-1,4-
182:
162:
144:
139:
135:
123:
111:
91:
79:
67:
55:
47:
42:
30:
25:
2920:Diffusion-limited enzyme
2543:Medical Subject Headings
2444:– LipOXygenases DataBase
909:Lipoxin § Synthesis
690:(12-HETE) or to various
16:Not to be confused with
2532:families/superfamily-87
2260:10.1126/science.8502991
890:– item 5 in the table).
888:Ichthyosis § Types
385:dihomo-Îł-linolenic acid
214:) are a family of (non-
2535:– animal lipoxygenases
1328:of the well-expressed
1291:kinetic isotope effect
1014:
508:
457:nonclassic eicosanoids
3013:Eadie–Hofstee diagram
2946:Allosteric regulation
2725:: two atoms of oxygen
2597:Non-heme iron protein
1523:10.3945/an.114.007732
1511:Advances in Nutrition
1012:
915:to resolvin D's (see
913:eicosapentaenoic acid
640:eicosapentaenoic acid
599:(5-HETE) and then to
502:
397:eicosapentaenoic acid
3023:Lineweaver–Burk plot
2813:: one atom of oxygen
2786:Cysteine dioxygenase
2776:Catechol dioxygenase
2664:Tyrosine hydroxylase
657:docosahexaenoic acid
486:hydroperoxide lyases
405:alpha-linolenic acid
401:docosahexaenoic acid
226:, more specifically
2654:Iron–sulfur protein
2295:10.1021/bi00131a022
2252:1993Sci...260.1482B
2246:(5113): 1482–1486.
1761:2006COPB....9..274M
1051:that provide three
923:Mouse lipoxygenases
512:Human lipoxygenases
463:Plant lipoxygenases
393:omega-3 fatty acids
373:omega 6 fatty acids
2982:Enzyme superfamily
2915:Enzyme promiscuity
2839:Inositol oxygenase
2820:Firefly luciferase
2801:Chlorite dismutase
2773:other dioxygenase:
2649:Inositol oxygenase
2453:2019-09-12 at the
2198:. 104–105: 84–92.
1940:10.1002/cbin.10345
1673:Annu. Rev. Biochem
1366:10.1002/prot.21590
1324:gene, which is an
1015:
961:cholesterol esters
901:Further metabolism
759:cholesterol esters
532:genes contain 14 (
509:
409:omega-9 fatty acid
3138:
3137:
2847:
2846:
2672:
2671:
2383:10.1021/ja502726s
2289:(16): 4053–4057.
1858:10.1021/cr200246d
1287:
1286:
787:-lipoxygenase, 12
783:), also termed 12
737:and possibly the
427:phospholipase A2s
228:oxidative enzymes
198:
197:
194:
193:
189:structure summary
3209:
3155:
3154:
3146:
3018:Hanes–Woolf plot
2961:Enzyme activator
2956:Enzyme inhibitor
2930:Enzyme catalysis
2874:
2867:
2860:
2851:
2850:
2699:
2692:
2685:
2676:
2675:
2616:Bacterioferritin
2589:Carrier proteins
2582:
2575:
2568:
2559:
2558:
2523:
2511:
2487:
2471:
2430:
2429:
2427:
2425:
2411:
2405:
2404:
2394:
2362:
2356:
2355:
2345:
2313:
2307:
2306:
2278:
2272:
2271:
2235:
2226:
2225:
2215:
2187:
2181:
2180:
2170:
2138:
2132:
2131:
2129:
2127:
2113:
2104:
2103:
2093:
2061:
2048:
2047:
2045:
2043:
2029:
2020:
2019:
2017:
2015:
2001:
1995:
1994:
1966:
1960:
1959:
1923:
1917:
1916:
1876:
1870:
1869:
1846:Chemical Reviews
1841:
1835:
1834:
1827:
1821:
1820:
1792:
1781:
1780:
1744:
1738:
1737:
1727:
1718:(5): 3755–3761.
1703:
1697:
1696:
1668:
1662:
1661:
1635:
1629:
1628:
1600:
1594:
1593:
1583:
1551:
1545:
1544:
1534:
1502:
1493:
1492:
1482:
1450:
1435:
1434:
1424:
1392:
1386:
1385:
1349:
1259:arachidonate + O
1227:arachidonate + O
1182:arachidonate + O
1137:arachidonate + O
1083:
1082:
590:arachidonic acid
377:arachidonic acid
230:, most of which
137:
136:
35:
23:
22:
3217:
3216:
3212:
3211:
3210:
3208:
3207:
3206:
3177:
3176:
3175:
3161:
3149:
3141:
3139:
3134:
3046:Oxidoreductases
3032:
3008:Enzyme kinetics
2996:
2992:List of enzymes
2965:
2934:
2905:Catalytic triad
2883:
2878:
2848:
2843:
2824:
2805:
2717:
2706:Oxidoreductases
2703:
2673:
2668:
2632:
2599:
2593:metalloproteins
2586:
2515:
2503:
2479:
2463:
2455:Wayback Machine
2438:
2433:
2423:
2421:
2413:
2412:
2408:
2377:(23): 8157–60.
2363:
2359:
2314:
2310:
2279:
2275:
2236:
2229:
2188:
2184:
2139:
2135:
2125:
2123:
2115:
2114:
2107:
2062:
2051:
2041:
2039:
2031:
2030:
2023:
2013:
2011:
2003:
2002:
1998:
1967:
1963:
1924:
1920:
1877:
1873:
1852:(10): 5866–98.
1842:
1838:
1829:
1828:
1824:
1793:
1784:
1745:
1741:
1704:
1700:
1669:
1665:
1658:
1636:
1632:
1601:
1597:
1552:
1548:
1503:
1496:
1451:
1438:
1393:
1389:
1350:
1346:
1342:
1262:
1238:
1234:
1231:= leukotriene A
1230:
1185:
1140:
1103:
1081:
1041:
1020:
925:
865:-trans-epoxy-11
838:-HpETE) to the
649:cytochrome P450
514:
465:
436:
336:
319:in four steps:
313:
294:
240:polyunsaturated
113:OPM superfamily
38:
21:
12:
11:
5:
3215:
3205:
3204:
3199:
3194:
3189:
3160:
3159:
3136:
3135:
3133:
3132:
3119:
3106:
3093:
3080:
3067:
3054:
3040:
3038:
3034:
3033:
3031:
3030:
3025:
3020:
3015:
3010:
3004:
3002:
2998:
2997:
2995:
2994:
2989:
2984:
2979:
2973:
2971:
2970:Classification
2967:
2966:
2964:
2963:
2958:
2953:
2948:
2942:
2940:
2936:
2935:
2933:
2932:
2927:
2922:
2917:
2912:
2907:
2902:
2897:
2891:
2889:
2885:
2884:
2877:
2876:
2869:
2862:
2854:
2845:
2844:
2842:
2841:
2835:
2833:
2826:
2825:
2823:
2822:
2816:
2814:
2807:
2806:
2804:
2803:
2798:
2793:
2788:
2783:
2778:
2769:
2768:
2763:
2754:
2749:
2740:
2728:
2726:
2719:
2718:
2710:monooxygenases
2702:
2701:
2694:
2687:
2679:
2670:
2669:
2667:
2666:
2661:
2656:
2651:
2646:
2640:
2638:
2634:
2633:
2631:
2630:
2625:
2620:
2619:
2618:
2607:
2605:
2601:
2600:
2585:
2584:
2577:
2570:
2562:
2556:
2555:
2546:
2536:
2525:
2513:
2501:
2477:
2461:
2445:
2437:
2436:External links
2434:
2432:
2431:
2406:
2357:
2308:
2273:
2227:
2182:
2133:
2105:
2049:
2021:
1996:
1961:
1918:
1871:
1836:
1822:
1803:(3): 390–400.
1782:
1755:(3): 274–280.
1739:
1698:
1663:
1656:
1630:
1595:
1546:
1494:
1436:
1387:
1360:(3): 1023–32.
1343:
1341:
1338:
1285:
1284:
1260:
1257:
1254:
1249:
1240:
1239:
1236:
1232:
1228:
1225:
1222:
1217:
1208:
1207:
1183:
1180:
1177:
1172:
1163:
1162:
1138:
1135:
1132:
1127:
1118:
1117:
1101:
1098:
1095:
1092:
1080:
1077:
1040:
1037:
1019:
1016:
1007:
1006:
996:
978:
974:
964:
946:
940:
924:
921:
892:
891:
820:
777:
766:
753:and/or to the
699:
664:
645:cyclooxygenase
624:leukotriene E4
620:leukotriene D4
616:leukotriene C4
612:leukotriene B4
608:leukotriene A4
513:
510:
505:linolenic acid
464:
461:
449:prostaglandins
435:
432:
352:, and various
342:
341:
338:
334:
331:
328:
311:
293:
290:
255:cell signaling
196:
195:
192:
191:
186:
180:
179:
166:
160:
159:
149:
142:
141:
133:
132:
127:
121:
120:
115:
109:
108:
95:
89:
88:
83:
77:
76:
71:
65:
64:
59:
53:
52:
49:
45:
44:
40:
39:
36:
28:
27:
9:
6:
4:
3:
2:
3214:
3203:
3200:
3198:
3195:
3193:
3190:
3188:
3185:
3184:
3182:
3174:
3170:
3166:
3158:
3153:
3148:
3147:
3144:
3130:
3126:
3125:
3120:
3117:
3113:
3112:
3107:
3104:
3100:
3099:
3094:
3091:
3087:
3086:
3081:
3078:
3074:
3073:
3068:
3065:
3061:
3060:
3055:
3052:
3048:
3047:
3042:
3041:
3039:
3035:
3029:
3026:
3024:
3021:
3019:
3016:
3014:
3011:
3009:
3006:
3005:
3003:
2999:
2993:
2990:
2988:
2987:Enzyme family
2985:
2983:
2980:
2978:
2975:
2974:
2972:
2968:
2962:
2959:
2957:
2954:
2952:
2951:Cooperativity
2949:
2947:
2944:
2943:
2941:
2937:
2931:
2928:
2926:
2923:
2921:
2918:
2916:
2913:
2911:
2910:Oxyanion hole
2908:
2906:
2903:
2901:
2898:
2896:
2893:
2892:
2890:
2886:
2882:
2875:
2870:
2868:
2863:
2861:
2856:
2855:
2852:
2840:
2837:
2836:
2834:
2831:
2827:
2821:
2818:
2817:
2815:
2812:
2808:
2802:
2799:
2797:
2794:
2792:
2789:
2787:
2784:
2782:
2779:
2777:
2774:
2771:
2770:
2767:
2764:
2762:
2758:
2755:
2753:
2750:
2748:
2744:
2741:
2739:
2736:
2734:
2730:
2729:
2727:
2724:
2720:
2715:
2711:
2707:
2700:
2695:
2693:
2688:
2686:
2681:
2680:
2677:
2665:
2662:
2660:
2657:
2655:
2652:
2650:
2647:
2645:
2642:
2641:
2639:
2635:
2629:
2626:
2624:
2621:
2617:
2614:
2613:
2612:
2609:
2608:
2606:
2602:
2598:
2594:
2590:
2583:
2578:
2576:
2571:
2569:
2564:
2563:
2560:
2554:
2550:
2547:
2544:
2540:
2537:
2534:
2533:
2529:
2526:
2522:
2518:
2514:
2510:
2506:
2502:
2499:
2495:
2491:
2486:
2482:
2478:
2475:
2470:
2466:
2462:
2460:
2456:
2452:
2449:
2446:
2443:
2440:
2439:
2420:
2416:
2410:
2402:
2398:
2393:
2388:
2384:
2380:
2376:
2372:
2368:
2361:
2353:
2349:
2344:
2339:
2335:
2331:
2328:(9): 1490–7.
2327:
2323:
2319:
2312:
2304:
2300:
2296:
2292:
2288:
2284:
2277:
2269:
2265:
2261:
2257:
2253:
2249:
2245:
2241:
2234:
2232:
2223:
2219:
2214:
2209:
2205:
2201:
2197:
2193:
2186:
2178:
2174:
2169:
2164:
2160:
2156:
2152:
2148:
2144:
2137:
2122:
2118:
2112:
2110:
2101:
2097:
2092:
2087:
2083:
2079:
2075:
2071:
2067:
2060:
2058:
2056:
2054:
2038:
2034:
2028:
2026:
2010:
2006:
2000:
1992:
1988:
1984:
1980:
1976:
1972:
1965:
1957:
1953:
1949:
1945:
1941:
1937:
1933:
1929:
1922:
1914:
1910:
1906:
1902:
1898:
1894:
1890:
1886:
1882:
1875:
1867:
1863:
1859:
1855:
1851:
1847:
1840:
1832:
1826:
1818:
1814:
1810:
1806:
1802:
1798:
1791:
1789:
1787:
1778:
1774:
1770:
1766:
1762:
1758:
1754:
1750:
1743:
1735:
1731:
1726:
1721:
1717:
1713:
1712:J. Biol. Chem
1709:
1702:
1694:
1690:
1686:
1682:
1678:
1674:
1667:
1659:
1657:9780126754094
1653:
1649:
1645:
1641:
1634:
1626:
1622:
1618:
1614:
1611:(4): 377–82.
1610:
1606:
1599:
1591:
1587:
1582:
1577:
1573:
1569:
1565:
1561:
1560:Redox Biology
1557:
1550:
1542:
1538:
1533:
1528:
1524:
1520:
1517:(5): 513–40.
1516:
1512:
1508:
1501:
1499:
1490:
1486:
1481:
1476:
1472:
1468:
1465:(4): 308–30.
1464:
1460:
1456:
1449:
1447:
1445:
1443:
1441:
1432:
1428:
1423:
1418:
1414:
1410:
1407:(4): 340–55.
1406:
1402:
1398:
1391:
1383:
1379:
1375:
1371:
1367:
1363:
1359:
1355:
1348:
1344:
1337:
1335:
1331:
1327:
1323:
1319:
1315:
1311:
1307:
1303:
1299:
1294:
1292:
1282:
1278:
1274:
1270:
1266:
1258:
1255:
1253:
1250:
1248:
1245:
1242:
1241:
1226:
1223:
1221:
1218:
1216:
1213:
1210:
1209:
1205:
1201:
1197:
1193:
1189:
1181:
1178:
1176:
1173:
1171:
1168:
1165:
1164:
1160:
1156:
1152:
1148:
1144:
1136:
1133:
1131:
1128:
1126:
1123:
1120:
1119:
1115:
1111:
1107:
1100:linoleate + O
1099:
1096:
1093:
1091:
1088:
1085:
1084:
1076:
1072:
1069:
1065:
1060:
1058:
1054:
1050:
1045:
1036:
1034:
1030:
1026:
1011:
1004:
1000:
997:
994:
990:
986:
982:
979:
975:
972:
968:
965:
962:
958:
954:
953:phospholipids
950:
947:
944:
941:
938:
935:
934:
933:
931:
920:
918:
914:
910:
906:
902:
898:
889:
885:
880:
876:
873:and 9-keto-10
872:
868:
864:
860:
856:
852:
848:
844:
843:stereoisomers
841:
837:
833:
829:
825:
821:
818:
814:
810:
806:
802:
798:
794:
790:
786:
782:
778:
775:
771:
767:
764:
760:
756:
752:
751:phospholipids
748:
744:
743:linoleic acid
740:
736:
732:
728:
724:
720:
719:
714:
710:
707:
703:
700:
697:
693:
689:
685:
684:
679:
675:
672:
668:
665:
662:
658:
654:
650:
646:
641:
637:
633:
629:
625:
621:
617:
613:
609:
606:
603:(5-oxo-ETE),
602:
598:
595:
591:
587:
586:
581:
577:
574:
570:
567:
566:
565:
563:
559:
555:
551:
547:
543:
539:
535:
531:
527:
523:
519:
506:
501:
497:
495:
491:
490:cis-3-hexenal
487:
483:
482:
477:
473:
470:
460:
458:
454:
450:
446:
442:
431:
428:
423:
421:
418:
414:
410:
406:
402:
398:
394:
390:
386:
382:
381:linoleic acid
378:
374:
369:
367:
363:
359:
355:
351:
347:
339:
332:
329:
326:
322:
321:
320:
318:
317:
316:hydroperoxide
314:→ fatty acid
307:
303:
299:
289:
287:
282:
281:derivatives.
280:
276:
270:
268:
264:
260:
256:
252:
248:
244:
241:
237:
236:dioxygenation
233:
229:
225:
221:
217:
213:
209:
206:
202:
201:Lipoxygenases
190:
187:
185:
181:
178:
174:
170:
167:
165:
161:
157:
153:
150:
147:
143:
138:
134:
131:
128:
126:
122:
119:
116:
114:
110:
107:
103:
99:
96:
94:
90:
87:
84:
82:
78:
75:
72:
70:
66:
63:
60:
58:
54:
50:
46:
41:
34:
29:
24:
19:
18:Lysyl oxidase
3124:Translocases
3121:
3108:
3095:
3082:
3069:
3059:Transferases
3056:
3043:
2900:Binding site
2772:
2733:lipoxygenase
2732:
2731:
2659:Lipoxygenase
2658:
2539:Lipoxygenase
2530:
2497:
2493:
2489:
2473:
2422:. Retrieved
2418:
2409:
2374:
2370:
2360:
2325:
2321:
2311:
2286:
2283:Biochemistry
2282:
2276:
2243:
2239:
2195:
2185:
2150:
2146:
2136:
2124:. Retrieved
2120:
2076:(3): 401–8.
2073:
2069:
2040:. Retrieved
2036:
2012:. Retrieved
2008:
1999:
1974:
1970:
1964:
1931:
1927:
1921:
1891:(1): 26–32.
1888:
1884:
1874:
1849:
1845:
1839:
1825:
1800:
1796:
1752:
1748:
1742:
1715:
1711:
1701:
1676:
1672:
1666:
1639:
1633:
1608:
1604:
1598:
1563:
1559:
1549:
1514:
1510:
1462:
1458:
1404:
1400:
1390:
1357:
1353:
1347:
1329:
1321:
1295:
1288:
1280:
1276:
1272:
1268:
1264:
1203:
1199:
1195:
1191:
1187:
1158:
1154:
1150:
1146:
1142:
1113:
1109:
1105:
1094:lipoxygenase
1073:
1061:
1046:
1042:
1021:
1018:3D structure
1002:
992:
988:
984:
970:
926:
903: and
893:
878:
874:
870:
866:
862:
858:
854:
850:
846:
839:
835:
831:
812:
804:
796:
792:
791:-LOX, and 12
788:
784:
763:lipoproteins
730:
722:
716:
681:
627:
622:and then to
604:
593:
583:
553:
549:
545:
541:
537:
533:
529:
521:
517:
515:
479:
466:
453:leukotrienes
437:
424:
416:
389:adrenic acid
370:
346:leukotrienes
343:
309:
295:
292:Biochemistry
283:
271:
222:-containing
211:
200:
199:
51:Lipoxygenase
26:Lipoxygenase
3197:Eicosanoids
2895:Active site
2644:Hemerythrin
2628:Transferrin
2623:Lactoferrin
2474:Glycine max
1934:(1): 3–22.
1566:: 297–310.
1039:Active site
1033:active site
1025:PLAT domain
957:cholesterol
801:sphingosine
755:cholesterol
526:kilodaltons
445:eicosanoids
358:peroxidases
302:beta barrel
300:N-terminal
243:fatty acids
125:OPM protein
43:Identifiers
3187:EC 1.13.11
3181:Categories
3098:Isomerases
3072:Hydrolases
2939:Regulation
1679:: 69–102.
1340:References
1334:pseudogene
1247:1.13.11.40
1215:1.13.11.34
1170:1.13.11.33
1125:1.13.11.31
1090:1.13.11.12
1068:asparagine
1066:oxygen of
1064:side chain
905:Activities
739:hepoxilins
709:1.13.11.33
704:(ALOX15) (
694:(also see
692:hepoxilins
674:1.13.11.31
669:(ALOX12) (
614:(LTB4) or
576:1.13.11.34
560:with exon/
472:1.13.11.12
407:; and the
350:hepoxilins
298:kilodalton
251:pentadiene
152:structures
3173:IPR001024
2977:EC number
2553:blanching
2322:Structure
1977:: 49–63.
1053:histidine
930:orthologs
828:hepoxilin
718:IPR001885
683:IPR001885
655:) and of
585:IPR001885
571:(ALOX5) (
548:) or 15 (
481:IPR001246
447:(such as
420:chirality
413:mead acid
325:methylene
267:endocrine
263:paracrine
259:autocrine
208:1.13.11.-
86:PDOC00077
74:IPR013819
3169:InterPro
3001:Kinetics
2925:Cofactor
2888:Activity
2611:Ferritin
2451:Archived
2424:17 April
2401:24884374
2352:22795085
2222:22951339
2177:22730527
2126:17 April
2100:24021977
2042:17 April
2014:17 April
1991:25895638
1956:10160642
1948:25052386
1913:45820130
1905:26655290
1866:21936577
1817:23954555
1777:16595187
1625:25218301
1590:26298204
1541:26374175
1489:25316652
1431:25449650
1382:40013415
1374:17847087
1354:Proteins
1326:ortholog
1322:ALOX12P2
1057:β-barrel
897:lipoxins
713:InterPro
678:InterPro
636:lipoxins
580:InterPro
476:InterPro
441:isozymes
279:hydroxyl
232:catalyze
169:RCSB PDB
69:InterPro
3192:Enzymes
3157:Biology
3111:Ligases
2881:Enzymes
2832:: other
2830:1.13.99
2811:1.13.12
2723:1.13.11
2637:nonheme
2459:PROSITE
2392:4188422
2343:5226221
2303:1567851
2268:8502991
2248:Bibcode
2240:Science
2213:3526691
2168:3392071
2091:4116325
1757:Bibcode
1734:7508918
1693:3017195
1581:4556770
1532:4561827
1480:4370320
1422:5710736
1330:Alox12P
1310:ALOX15B
1302:ALOX12B
1186:= (5
1049:Ď€-helix
981:Alox12b
967:Alox15b
819:(ARCI).
809:carboxy
781:ALOX12B
770:ALOX15B
757:, i.e.
715::
680::
582::
550:ALOX12B
546:ALOX15B
478::
286:archaea
275:epoxide
224:enzymes
81:PROSITE
62:PF00305
3143:Portal
3085:Lyases
2761:ALOX15
2747:ALOX12
2545:(MeSH)
2442:LOX-DB
2399:
2389:
2350:
2340:
2301:
2266:
2220:
2210:
2175:
2165:
2098:
2088:
1989:
1954:
1946:
1911:
1903:
1864:
1815:
1775:
1732:
1691:
1654:
1623:
1588:
1578:
1539:
1529:
1487:
1477:
1429:
1419:
1380:
1372:
1318:ALOXE3
1316:, and
1306:ALOX15
1298:ALOX12
1141:= (5
999:Aloxe3
959:(i.e.
949:Alox15
943:Alox12
824:ALOXE3
626:), or
562:intron
554:ALOXE3
542:ALOX15
538:ALOX12
492:, the
403:, and
391:; the
387:, and
247:lipids
184:PDBsum
158:
148:
106:SUPFAM
48:Symbol
3037:Types
2716:1.13)
2147:Blood
1952:S2CID
1909:S2CID
1378:S2CID
1314:ALOX5
937:Alox5
761:, in
647:, or
558:exons
534:ALOX5
518:ALOX5
366:HODEs
253:into
102:SCOPe
93:SCOP2
3167:and
3165:Pfam
3129:list
3122:EC7
3116:list
3109:EC6
3103:list
3096:EC5
3090:list
3083:EC4
3077:list
3070:EC3
3064:list
3057:EC2
3051:list
3044:EC1
2604:heme
2521:3RDE
2509:1LOX
2485:1IK3
2469:1YGE
2426:2018
2397:PMID
2348:PMID
2299:PMID
2264:PMID
2218:PMID
2173:PMID
2128:2018
2096:PMID
2074:1841
2044:2018
2016:2018
1987:PMID
1944:PMID
1901:PMID
1862:PMID
1813:PMID
1801:1841
1773:PMID
1730:PMID
1689:PMID
1652:ISBN
1621:PMID
1609:1851
1586:PMID
1537:PMID
1485:PMID
1463:1851
1427:PMID
1405:1851
1370:PMID
1263:= (5
1104:= (9
1029:Pfam
955:and
861:),13
805:sn-2
455:and
364:and
234:the
220:iron
216:heme
177:PDBj
173:PDBe
156:ECOD
146:Pfam
130:2p0m
98:2sbl
57:Pfam
2517:PDB
2505:PDB
2496:,13
2492:,11
2481:PDB
2465:PDB
2457:in
2387:PMC
2379:doi
2375:136
2338:PMC
2330:doi
2291:doi
2256:doi
2244:260
2208:PMC
2200:doi
2163:PMC
2155:doi
2151:119
2086:PMC
2078:doi
1979:doi
1975:760
1936:doi
1893:doi
1854:doi
1850:111
1805:doi
1765:doi
1720:doi
1716:269
1681:doi
1644:doi
1613:doi
1576:PMC
1568:doi
1527:PMC
1519:doi
1475:PMC
1467:doi
1417:PMC
1409:doi
1362:doi
1279:,14
1275:,11
1235:+ H
1202:,15
1198:,13
1194:,11
1157:,14
1153:,12
1149:,10
1112:,13
1108:,11
919:).
877:,12
869:,13
857:(10
530:LOX
522:LOX
245:in
238:of
212:LOX
210:) (
164:PDB
3183::
3171::
2714:EC
2708::
2595::
2591:,
2519::
2507::
2483::
2467::
2417:.
2395:.
2385:.
2373:.
2369:.
2346:.
2336:.
2326:20
2324:.
2320:.
2297:.
2287:31
2285:.
2262:.
2254:.
2242:.
2230:^
2216:.
2206:.
2194:.
2171:.
2161:.
2149:.
2145:.
2119:.
2108:^
2094:.
2084:.
2072:.
2068:.
2052:^
2035:.
2024:^
2007:.
1985:.
1973:.
1950:.
1942:.
1932:39
1930:.
1907:.
1899:.
1889:27
1887:.
1883:.
1860:.
1848:.
1811:.
1799:.
1785:^
1771:.
1763:.
1751:.
1728:.
1714:.
1710:.
1687:.
1677:55
1675:.
1650:.
1619:.
1607:.
1584:.
1574:.
1562:.
1558:.
1535:.
1525:.
1513:.
1509:.
1497:^
1483:.
1473:.
1461:.
1457:.
1439:^
1425:.
1415:.
1403:.
1399:.
1376:.
1368:.
1358:70
1356:.
1312:,
1308:,
1304:,
1300:,
1271:,9
1267:,8
1244:EC
1212:EC
1190:,8
1167:EC
1145:,8
1122:EC
1087:EC
731:2)
723:1)
711:;
706:EC
698:).
676:;
671:EC
634:,
628:3)
605:2)
594:1)
578:;
573:EC
556:)
552:,
544:,
540:,
536:,
496:.
474:;
469:EC
451:,
411:,
399:,
395:,
383:,
379:,
375:,
348:,
277:,
218:)
205:EC
175:;
171:;
154:/
118:80
104:/
100:/
3145::
3131:)
3127:(
3118:)
3114:(
3105:)
3101:(
3092:)
3088:(
3079:)
3075:(
3066:)
3062:(
3053:)
3049:(
2873:e
2866:t
2859:v
2759:/
2745:/
2735::
2712:(
2698:e
2691:t
2684:v
2581:e
2574:t
2567:v
2498:S
2494:E
2490:Z
2476:)
2428:.
2403:.
2381::
2354:.
2332::
2305:.
2293::
2270:.
2258::
2250::
2224:.
2202::
2179:.
2157::
2130:.
2102:.
2080::
2046:.
2018:.
1993:.
1981::
1958:.
1938::
1915:.
1895::
1868:.
1856::
1833:.
1819:.
1807::
1779:.
1767::
1759::
1753:9
1736:.
1722::
1695:.
1683::
1660:.
1646::
1627:.
1615::
1592:.
1570::
1564:6
1543:.
1521::
1515:6
1491:.
1469::
1433:.
1411::
1384:.
1364::
1281:Z
1277:Z
1273:E
1269:R
1265:Z
1261:2
1237:2
1233:4
1229:2
1204:S
1200:E
1196:Z
1192:Z
1188:Z
1184:2
1159:Z
1155:S
1151:E
1147:Z
1143:Z
1139:2
1114:S
1110:E
1106:Z
1102:2
1003:R
993:R
989:R
985:R
971:S
879:Z
875:E
871:R
867:E
863:R
859:R
855:R
851:R
847:R
840:R
836:S
832:S
813:R
797:R
793:R
789:R
785:R
417:S
335:2
312:2
203:(
20:.
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
