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Literature summary extracted from

  • Ollmann, I.R.; Hogg, J.H.; Munoz, B.; Haeggstrom, J.Z.; Samuelsson, B.; Wong, C.H.
    Investigation of the inhibition of leukotriene A4 hydrolase (1995), Bioorg. Med. Chem., 3, 969-995.
    View publication on PubMed

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 Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.3.2.6 (2S)-2-amino-3-[4-(benzyloxy)phenyl]propane-1-thiol it are about 50 derivates and related structures synthesized and assayed their inhibition of enzyme catalyzes hxdrolysis of L-alanine-4-nitroanilide Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.3.2.6 Zinc zinc protein Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
3.3.2.6 Mus musculus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanism Mus musculus
3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.3.2.6 leukotriene A4 + H2O
-
Mus musculus leukotriene B4
-
?
3.3.2.6 additional information
-
Mus musculus ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.3.2.6 0.7
-
leukotriene A4
-
Mus musculus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.3.2.6 additional information
-
additional information
-
Mus musculus
3.3.2.6 0.046
-
2-oxo-3-amino carboxylic ester
-
Mus musculus