3.3.2.6 (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O - Mus musculus (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate - ? 393911 3.3.2.6 (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O - Homo sapiens (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate - ? 393911 3.3.2.6 (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O - Cricetulus sp. (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate - ? 393911 3.3.2.6 (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O substrate for epoxide hydrolase activity Saccharomyces cerevisiae (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate - ? 393911 3.3.2.6 (7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O substrate for the epoxide hydrolase reaction, in addition LTA4H shows a peptidase activity Homo sapiens (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate - ? 393911 3.3.2.6 Ala-4-nitroanilide + H2O - Homo sapiens Ala + 4-nitroaniline - ? 36589 3.3.2.6 Arg-Ala-Arg + H2O - Homo sapiens ? - ? 404352 3.3.2.6 Arg-Ser-Arg + H2O - Homo sapiens ? - ? 404359 3.3.2.6 L-Ala-4-nitroanilide + H2O - Homo sapiens L-Ala + 4-nitroaniline - ? 382096 3.3.2.6 L-Ala-4-nitroanilide + H2O aminopeptidase activity Mus musculus L-Ala + 4-nitroaniline - ? 382096 3.3.2.6 L-Ala-p-nitroanilide + H2O - Homo sapiens L-Ala + p-nitroaniline - ? 381360 3.3.2.6 L-alanine 2-naphthylamide + H2O - Saccharomyces cerevisiae L-alanine + 2-naphthylamine - ? 417131 3.3.2.6 L-alanine-4-nitroanilide + H2O - Mus musculus L-alanine + 4-nitroaniline - ? 364854 3.3.2.6 L-alanine-4-nitroanilide + H2O - Homo sapiens L-alanine + 4-nitroaniline - ? 364854 3.3.2.6 L-alanine-4-nitroanilide + H2O - Xenopus laevis L-alanine + 4-nitroaniline - ? 364854 3.3.2.6 L-alanine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-alanine + 7-amino-4-methylcoumarin - ? 431991 3.3.2.6 L-Arg-L-Ala-L-Arg + H2O bi-functional enzyme that also exhibits aminopeptidase activity with a preference over arginyl tripeptides Homo sapiens ? - ? 431999 3.3.2.6 L-Arg-p-nitroanilide + H2O - Homo sapiens L-Arg + p-nitroaniline - ? 36321 3.3.2.6 L-arginine + H2O the best proteinogenic amino acid recognized by the enzyme is L-arginine Homo sapiens ? - ? 369827 3.3.2.6 L-arginine 2-naphthylamide + H2O - Saccharomyces cerevisiae L-arginine + 2-naphthylamine - ? 417137 3.3.2.6 L-arginine-4-nitroanilide + H2O - Homo sapiens L-arginine + 4-nitroaniline - ? 418749 3.3.2.6 L-arginine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-arginine + 7-amino-4-methylcoumarin - ? 432003 3.3.2.6 L-arginine-7-amido-4-methylcoumarine + H2O an artificial substrate Homo sapiens L-arginine + 4-methylcoumarin-7-amine - ? 450139 3.3.2.6 L-glutamate-7-amido-4-methylcoumarin + H2O - Homo sapiens L-glutamate + 7-amino-4-methylcoumarin - ? 432015 3.3.2.6 L-histidine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-histidine + 7-amino-4-methylcoumarin - ? 432022 3.3.2.6 L-isoleucine 2-naphthylamide + H2O - Saccharomyces cerevisiae L-isoleucine + 2-naphthylamine - ? 417157 3.3.2.6 L-leucine 2-naphthylamide + H2O - Saccharomyces cerevisiae L-leucine + 2-naphthylamine - ? 417161 3.3.2.6 L-leucine-4-nitroanilide + H2O - Homo sapiens L-leucine + 4-nitroaniline - ? 364849 3.3.2.6 L-leucine-4-nitroanilide + H2O - Saccharomyces cerevisiae L-leucine + 4-nitroaniline - ? 364849 3.3.2.6 L-leucine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-leucine + 7-amino-4-methylcoumarin - ? 418764 3.3.2.6 L-lysine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-lysine + 7-amino-4-methylcoumarin - ? 432039 3.3.2.6 L-methionine 2-naphthylamide + H2O - Saccharomyces cerevisiae L-methionine + 2-naphthylamine - ? 417168 3.3.2.6 L-methionine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-methionine + 7-amino-4-methylcoumarin - ? 392396 3.3.2.6 L-phenylalanine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-phenylalanine + 7-amino-4-methylcoumarin - ? 432048 3.3.2.6 L-Pro-Gly-L-Pro + H2O - Homo sapiens ? - ? 432049 3.3.2.6 L-proline-7-amido-4-methylcoumarin + H2O - Homo sapiens L-proline + 7-amino-4-methylcoumarin - ? 412328 3.3.2.6 L-serine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-serine + 7-amino-4-methylcoumarin - ? 432053 3.3.2.6 L-tyrosine-7-amido-4-methylcoumarin + H2O - Homo sapiens L-tyrosine + 7-amino-4-methylcoumarin - ? 432058 3.3.2.6 L-Val-4-nitroanilide + H2O - Homo sapiens L-Val + 4-nitroaniline - ? 382188 3.3.2.6 L-valine 2-naphthylamide + H2O - Saccharomyces cerevisiae L-valine + 2-naphthylamine - ? 417206 3.3.2.6 leukotriene A4 + H2O - Cavia porcellus leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Mus musculus leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Homo sapiens leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Rattus norvegicus leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Canis lupus familiaris leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Xenopus laevis leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Danio rerio leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Canis lupus familiaris leukotriene B4 i.e. LTB4, a potent inflammatory mediator originating from membrane-derived arachidonic acid ? 361325 3.3.2.6 leukotriene A4 + H2O - Homo sapiens leukotriene B4 i.e. LTB4, a powerful proinflammatory agent ? 361325 3.3.2.6 leukotriene A4 + H2O - Mus musculus leukotriene B4 LTB4 is an endogenous itch mediator in the skin and is involved in the pruritus response in allergic reactions ? 361325 3.3.2.6 leukotriene A4 + H2O highly specific Rattus norvegicus leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O i.e. 5(S)-trans-5,6-oxido-7,9-trans-11,14-cis-eicosatetraenoic acid Cavia porcellus leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Saccharomyces cerevisiae leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Xenopus laevis leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Cavia porcellus leukotriene B4 mutants of Tyr378 are able to generate, not only leukotriene B4, but also (5S,12R)-dihydroxy-6,10-trans-8,14-cis-eicosatetraenoic acid, in a yield of about 20-30% ? 361325 3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Mus musculus leukotriene B4 mutants of Tyr378 are able to generate, not only leukotriene B4, but also (5S,12R)-dihydroxy-6,10-trans-8,14-cis-eicosatetraenoic acid, in a yield of about 20-30% ? 361325 3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Homo sapiens leukotriene B4 mutants of Tyr378 are able to generate, not only leukotriene B4, but also (5S,12R)-dihydroxy-6,10-trans-8,14-cis-eicosatetraenoic acid, in a yield of about 20-30% ? 361325 3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Rattus norvegicus leukotriene B4 mutants of Tyr378 are able to generate, not only leukotriene B4, but also (5S,12R)-dihydroxy-6,10-trans-8,14-cis-eicosatetraenoic acid, in a yield of about 20-30% ? 361325 3.3.2.6 leukotriene A4 + H2O one of the physiologically important processes in the arachidonic acid biosynthetic pathway, leukotriene B4 is a proinflammatory mediator which stimulates adhesion of circulating neutrophils to vascular endothelium and directs their migration towards sites of inflammation Homo sapiens leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O central enzyme in leukotriene B4 formation, it is likely to be involved in transcellular leukotriene formation Homo sapiens leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O biosynthesis of leukotriene B4 Homo sapiens leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O biosynthesis of leukotriene B4 Rattus norvegicus leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O biosynthesis of leukotriene B4 Cavia porcellus leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O leukotriene A4 hydrolase catalyzes the final step in the synthesis of leukotriene B4, a potent chemoattractant and proinflammatory eicosanoid Homo sapiens leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O leukotriene A4 hydrolase catalyzes the final step in the synthesis of leukotriene B4, a potent chemoattractant and proinflammatory eicosanoid. LTB4 functions as a macrophage chemoattractant in the zebrafish, injection into the hindbrain ventricle of wild-type arvae induces rapid recruitment of macrophages Danio rerio leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O LTA4 Homo sapiens leukotriene B4 LTB4 ? 361325 3.3.2.6 leukotriene A4 + H2O - Mus musculus C57BL/6 leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Mus musculus C57BL/6J leukotriene B4 - ? 361325 3.3.2.6 leukotriene A4 + H2O - Saccharomyces cerevisiae (5S,6S)-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic acid i.e. DHETE ? 361334 3.3.2.6 leukotriene A4 + H2O - Xenopus laevis leukotriene B4 + (5S,12R)-dihydroxy-6,10-trans-8,14,cis-eicosatetraenoic acid 90% leukotriene B4 and 10% (5S,12R)-dihydroxy-6,10-trans-8,14,cis-eicosatetraenoic acid ? 361335 3.3.2.6 leukotriene A4 + H2O - Saccharomyces cerevisiae (5S,6S)-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic acid + leukotriene B4 + (5S,12R)-dihydroxy-6,10-trans-8,14,cis-eicosatetraenoic acid when large amounts of enzyme are incubated with leukotriene A4: 72% (5S,6S)-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic acid, 18% leukotriene B4 and 10% (5S,12R)-dihydroxy-6,10-trans-8,14,cis-eicosatetraenoic acid ? 361336 3.3.2.6 leukotriene A4 + H2O - Xenopus laevis leukotriene B4 + 5(S),12R-dihydroxy-6,10-trans-8,14-ciseicosatetraenoic acid product ratio 9:1 ? 431052 3.3.2.6 leukotriene A5 + H2O i.e. 5(S)-trans-5,6-oxido-7,9-trans-11,14,17-cis-eicosatetraenoic acid Homo sapiens ? - ? 361326 3.3.2.6 leukotriene A5 + H2O i.e. 5(S)-trans-5,6-oxido-7,9-trans-11,14,17-cis-eicosatetraenoic acid Rattus norvegicus ? - ? 361326 3.3.2.6 lysine-4-nitroanilide + H2O - Homo sapiens lysine + 4-nitroaniline - ? 361331 3.3.2.6 additional information - Cavia porcellus ? - ? 89 3.3.2.6 additional information - Mus musculus ? - ? 89 3.3.2.6 additional information - Homo sapiens ? - ? 89 3.3.2.6 additional information - Saccharomyces cerevisiae ? - ? 89 3.3.2.6 additional information - Xenopus laevis ? - ? 89 3.3.2.6 additional information - Caenorhabditis elegans ? - ? 89 3.3.2.6 additional information neutrophil LTA4 hydrolase also converts LTA5 to LTB5, less efficiently than LTA4 to LTB4 Homo sapiens ? - ? 89 3.3.2.6 additional information either glutamic or glutamine moiety at amino acid 297 is required for full LTA4 hydrolase activity, free carboxylic acid of glutamic acid is essential for aminopeptidase Homo sapiens ? - ? 89 3.3.2.6 additional information not: glycine-4-nitroanilide, glutamyl-4-nitroanilide, valine-4-nitroanilide Homo sapiens ? - ? 89 3.3.2.6 additional information the aminopeptidase activity accepts a variety of substrates and certain arginyl di- and tri-peptides as well as p-nitroanilide derivates of Ala and Arg Cavia porcellus ? - ? 89 3.3.2.6 additional information the aminopeptidase activity accepts a variety of substrates and certain arginyl di- and tri-peptides as well as p-nitroanilide derivates of Ala and Arg Mus musculus ? - ? 89 3.3.2.6 additional information the aminopeptidase activity accepts a variety of substrates and certain arginyl di- and tri-peptides as well as p-nitroanilide derivates of Ala and Arg Homo sapiens ? - ? 89 3.3.2.6 additional information the aminopeptidase activity accepts a variety of substrates and certain arginyl di- and tri-peptides as well as p-nitroanilide derivates of Ala and Arg Rattus norvegicus ? - ? 89 3.3.2.6 additional information possible proteolytic function of the enzyme may be limited to the extracellular space Homo sapiens ? - ? 89 3.3.2.6 additional information LTA4H is a zinc metalloprotease Homo sapiens ? - ? 89 3.3.2.6 additional information LTA4H is a zinc metalloprotease Rattus norvegicus ? - ? 89 3.3.2.6 additional information LTA4H is a zinc metalloprotease Canis lupus familiaris ? - ? 89 3.3.2.6 additional information no activity with L-Asn, L-Asp, L-Glu, Gly, L-Ile, L-Thr, L-Trp, L-Val, as well as D-amino acids Homo sapiens ? - ? 89 3.3.2.6 additional information proline-glycine-proline (PGP) is a substrate for the enzyme's aminopeptidase (AP) activity Rattus norvegicus ? - ? 89 3.3.2.6 additional information proline-glycine-proline (PGP) is a substrate for the enzyme's aminopeptidase (AP) activity Homo sapiens ? - ? 89 3.3.2.6 additional information substrates docking and molecular dynamics simulations, interaction analysis. The binding cavity of LTA4H is formed by H299, H295, E318, and Zn2+. Residues R563 and K565 in the C-terminal domain of LTA4H are key residues involved in carboxylate recognition from endogenous substrates of the enzyme Homo sapiens ? - ? 89 3.3.2.6 additional information the aminopeptidase binding site shares a similar structure to LTA4H at its ligand binding sites Homo sapiens ? - ? 89 3.3.2.6 additional information the aminopeptidase binding site shares a similar structure to LTA4H at its ligand binding sites Mus musculus ? - ? 89 3.3.2.6 proline-4-nitroanilide + H2O - Homo sapiens proline + 4-nitroaniline - ? 361329 3.3.2.6 proline-glycine-proline + H2O PGP Homo sapiens ? - ? 450514