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Literature summary extracted from

  • Kull, F.; Ohlson, E.; Haeggstrom, J.Z.
    Cloning and characterization of a bifunctional leukotriene A4 hydrolase from Saccharomyces cerevisiae (1999), J. Biol. Chem., 274, 34683-34690.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.3.2.6 leukotriene A4 stimulates strong aminopeptidase activity via lipid binding site Saccharomyces cerevisiae

Application

EC Number Application Comment Organism
3.3.2.6 medicine the enzyme catalyses the hydrolysis of leukotriene A4 into the proinflammatory substance leukotriene B4 Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.3.2.6 expression in Escherichia coli and in Sf9 cells, using the baculovirus system Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.3.2.6 bestatin
-
 Homo sapiens
3.3.2.6 bestatin aminopeptidase activity, leukotriene A4 competes partially Saccharomyces cerevisiae
3.3.2.6 hydroxamic acid aminopeptidase activity Saccharomyces cerevisiae
3.3.2.6 leukotriene A4 leukotriene A4 binds covalently to Tyr378 and blocks epoxide hydrolase and aminopeptidase activities Homo sapiens
3.3.2.6 leukotriene A4 inhibits epoxid hydrolase activity and stimulates peptidase activity Saccharomyces cerevisiae
3.3.2.6 thioamine
-
 Homo sapiens
3.3.2.6 thioamine aminopeptidase activity, leukotriene A4 restores Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.3.2.6 0.15
-
 L-leucine-4-nitroanilide pH 7.5, 22°C Homo sapiens
3.3.2.6 1.5
-
 L-leucine-4-nitroanilide pH 7.5, 22°C Saccharomyces cerevisiae
3.3.2.6 2
-
 L-leucine-4-nitroanilide pH 7.5, 22°C, enzyme stimulated by leukotriene A4 Saccharomyces cerevisiae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.3.2.6 Zinc zinc protein Homo sapiens
3.3.2.6 Zinc zinc protein Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.3.2.6 72000
-
 x * 72000, SDS-PAGE Saccharomyces cerevisiae

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
-
 leukotriene B4
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.6 Caenorhabditis elegans
-
-
-
3.3.2.6 Homo sapiens
-
-
-
3.3.2.6 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.3.2.6 recombinant enzyme Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Homo sapiens
a
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.6 L-leucine-4-nitroanilide + H2O
-
 Homo sapiens L-leucine + 4-nitroaniline
-
 ?
3.3.2.6 L-leucine-4-nitroanilide + H2O
-
 Saccharomyces cerevisiae L-leucine + 4-nitroaniline
-
 ?
3.3.2.6 leukotriene A4 + H2O
-
 Homo sapiens leukotriene B4
-
 ?
3.3.2.6 leukotriene A4 + H2O
-
 Saccharomyces cerevisiae (5S,6S)-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic acid i.e. DHETE ?
3.3.2.6 additional information
-
 Homo sapiens ?
-
 ?
3.3.2.6 additional information
-
 Saccharomyces cerevisiae ?
-
 ?
3.3.2.6 additional information
-
 Caenorhabditis elegans ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.3.2.6 ?
-
 Homo sapiens
3.3.2.6 ? x * 72000, SDS-PAGE Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.3.2.6 0.35
-
 L-leucine-4-nitroanilide pH 7.5, 22°C Homo sapiens
3.3.2.6 0.63
-
 L-leucine-4-nitroanilide pH 7.5, 22°C Saccharomyces cerevisiae
3.3.2.6 5.2
-
 L-leucine-4-nitroanilide pH 7.5, 22°C, enzyme stimulated by leukotriene A4 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.3.2.6 7.3
-
-
 Saccharomyces cerevisiae