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Literature summary for 3.3.2.6 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
Search for more literature for 3.3.2.6

Activating Compound

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

Application

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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
leukotriene A4 + H2O Homo sapiens
-
 leukotriene B4
-
 ?

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Saccharomyces cerevisiae

Reaction

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

Substrates and Products (Substrate)

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

Subunits

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
 Saccharomyces cerevisiae