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Literature summary extracted from

  • Haeggstrom, J.Z.; Kull, F.; Rudberg, P.C.; Tholander, F.; Thunnissen, M.M.
    Leukotriene A4 hydrolase (2002), Prostaglandins, 68-69, 495-510.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.3.2.6 albumin stimulates aminopeptidase activity Cavia porcellus
3.3.2.6 albumin stimulates aminopeptidase activity Mus musculus
3.3.2.6 albumin stimulates aminopeptidase activity Homo sapiens
3.3.2.6 albumin stimulates aminopeptidase activity Rattus norvegicus
3.3.2.6 Br- stimulates aminopeptidase activity Cavia porcellus
3.3.2.6 Br- stimulates aminopeptidase activity Mus musculus
3.3.2.6 Br- stimulates aminopeptidase activity Homo sapiens
3.3.2.6 Br- stimulates aminopeptidase activity Rattus norvegicus
3.3.2.6 Cl- stimulates aminopeptidase activity Cavia porcellus
3.3.2.6 Cl- stimulates aminopeptidase activity Mus musculus
3.3.2.6 Cl- stimulates aminopeptidase activity Homo sapiens
3.3.2.6 Cl- stimulates aminopeptidase activity Rattus norvegicus
3.3.2.6 leukotriene A4
-
Saccharomyces cerevisiae
3.3.2.6 SCN- stimulates aminopeptidase activity Cavia porcellus
3.3.2.6 SCN- stimulates aminopeptidase activity Mus musculus
3.3.2.6 SCN- stimulates aminopeptidase activity Homo sapiens
3.3.2.6 SCN- stimulates aminopeptidase activity Rattus norvegicus

Application

EC Number Application Comment Organism
3.3.2.6 medicine the product is a classical chemoattractant, triggers adherence and aggregation of leukocytes to the endothelium, modulates immune responses, participates in the host-defence against infections and is a mediator of PAF-induced lethal shock Cavia porcellus
3.3.2.6 medicine the product is a classical chemoattractant, triggers adherence and aggregation of leukocytes to the endothelium, modulates immune responses, participates in the host-defence against infections and is a mediator of PAF-induced lethal shock Mus musculus
3.3.2.6 medicine the product is a classical chemoattractant, triggers adherence and aggregation of leukocytes to the endothelium, modulates immune responses, participates in the host-defence against infections and is a mediator of PAF-induced lethal shock Homo sapiens
3.3.2.6 medicine the product is a classical chemoattractant, triggers adherence and aggregation of leukocytes to the endothelium, modulates immune responses, participates in the host-defence against infections and is a mediator of PAF-induced lethal shock Rattus norvegicus
3.3.2.6 medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Cavia porcellus
3.3.2.6 medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Mus musculus
3.3.2.6 medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Homo sapiens
3.3.2.6 medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.3.2.6 crystal structure of enzyme complexed with bestatin Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.3.2.6 2-oxo-3-amino carboxylic esters
-
Cavia porcellus
3.3.2.6 2-oxo-3-amino carboxylic esters
-
Homo sapiens
3.3.2.6 2-oxo-3-amino carboxylic esters
-
Mus musculus
3.3.2.6 2-oxo-3-amino carboxylic esters
-
Rattus norvegicus
3.3.2.6 2-oxo-3-amino carboxylic esters
-
Saccharomyces cerevisiae
3.3.2.6 2-[4-[4-[2-[1-pyrrolidinyl]ethoxy]phenoxy]phenyl]-oxazole
-
Homo sapiens
3.3.2.6 bestatin
-
Cavia porcellus
3.3.2.6 bestatin
-
Homo sapiens
3.3.2.6 bestatin
-
Mus musculus
3.3.2.6 bestatin
-
Rattus norvegicus
3.3.2.6 bestatin
-
Saccharomyces cerevisiae
3.3.2.6 bestatin
-
Xenopus laevis
3.3.2.6 captopril
-
Cavia porcellus
3.3.2.6 captopril
-
Homo sapiens
3.3.2.6 captopril
-
Mus musculus
3.3.2.6 captopril
-
Rattus norvegicus
3.3.2.6 captopril
-
Saccharomyces cerevisiae
3.3.2.6 Kelatorphan
-
Cavia porcellus
3.3.2.6 Kelatorphan
-
Homo sapiens
3.3.2.6 Kelatorphan
-
Mus musculus
3.3.2.6 Kelatorphan
-
Rattus norvegicus
3.3.2.6 Kelatorphan
-
Saccharomyces cerevisiae
3.3.2.6 leukotriene A4
-
Cavia porcellus
3.3.2.6 leukotriene A4
-
Homo sapiens
3.3.2.6 leukotriene A4
-
Mus musculus
3.3.2.6 leukotriene A4
-
Rattus norvegicus
3.3.2.6 methyl-N-[3-[4-(phenylmethyl)-phenoxy]propyl]-beta-alanine
-
Homo sapiens
3.3.2.6 thioamine
-
Cavia porcellus
3.3.2.6 thioamine
-
Homo sapiens
3.3.2.6 thioamine
-
Mus musculus
3.3.2.6 thioamine
-
Rattus norvegicus
3.3.2.6 thioamine
-
Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.3.2.6 additional information
-
Homo sapiens
-
-
3.3.2.6 additional information
-
Rattus norvegicus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.3.2.6 Zinc catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318 Cavia porcellus
3.3.2.6 Zinc catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318 Mus musculus
3.3.2.6 Zinc catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318 Homo sapiens
3.3.2.6 Zinc catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318 Rattus norvegicus
3.3.2.6 Zinc zinc content: 1 mol of zinc per mol of enzyme Mus musculus
3.3.2.6 Zinc zinc content: 1 mol of zinc per mol of enzyme Homo sapiens
3.3.2.6 Zinc zinc protein Cavia porcellus
3.3.2.6 Zinc zinc protein Mus musculus
3.3.2.6 Zinc zinc protein Homo sapiens
3.3.2.6 Zinc zinc protein Saccharomyces cerevisiae
3.3.2.6 Zinc zinc protein Xenopus laevis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.3.2.6 leukotriene A4 + H2O Homo sapiens biosynthesis of leukotriene B4 leukotriene B4
-
?
3.3.2.6 leukotriene A4 + H2O Rattus norvegicus biosynthesis of leukotriene B4 leukotriene B4
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.6 Cavia porcellus
-
-
-
3.3.2.6 Homo sapiens
-
-
-
3.3.2.6 Mus musculus
-
-
-
3.3.2.6 Rattus norvegicus
-
-
-
3.3.2.6 Saccharomyces cerevisiae
-
-
-
3.3.2.6 Xenopus laevis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 His295, His299, Glu318, Glu271 are amino acids involved in metallic binding and epoxid hydrolase activity, additional Glu296 and Tyr383 are required for the aminopeptidase activity Cavia porcellus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 His295, His299, Glu318, Glu271 are amino acids involved in metallic binding and epoxid hydrolase activity, additional Glu296 and Tyr383 are required for the aminopeptidase activity Mus musculus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 His295, His299, Glu318, Glu271 are amino acids involved in metallic binding and epoxid hydrolase activity, additional Glu296 and Tyr383 are required for the aminopeptidase activity Homo sapiens
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 His295, His299, Glu318, Glu271 are amino acids involved in metallic binding and epoxid hydrolase activity, additional Glu296 and Tyr383 are required for the aminopeptidase activity Rattus norvegicus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanistic models, Glu271 is specifically required for the epoxid hydrolase activity and peptidase activity Cavia porcellus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanistic models, Glu271 is specifically required for the epoxid hydrolase activity and peptidase activity Mus musculus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanistic models, Glu271 is specifically required for the epoxid hydrolase activity and peptidase activity Homo sapiens
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanistic models, Glu271 is specifically required for the epoxid hydrolase activity and peptidase activity Rattus norvegicus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanistic models, Glu271 is specifically required for the epoxid hydrolase activity and peptidase activity Saccharomyces cerevisiae
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Cavia porcellus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Mus musculus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Homo sapiens
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Rattus norvegicus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Saccharomyces cerevisiae
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Xenopus laevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Saccharomyces cerevisiae leukotriene B4
-
?
3.3.2.6 leukotriene A4 + H2O model for the binding of leukotriene A4 to the active site Xenopus laevis leukotriene B4
-
?
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% ?
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% ?
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% ?
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% ?
3.3.2.6 leukotriene A4 + H2O biosynthesis of leukotriene B4 Homo sapiens leukotriene B4
-
?
3.3.2.6 leukotriene A4 + H2O biosynthesis of leukotriene B4 Rattus norvegicus leukotriene B4
-
?
3.3.2.6 additional information
-
Saccharomyces cerevisiae ?
-
?
3.3.2.6 additional information
-
Xenopus laevis ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?