EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
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 |
- |
? |
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 |
- |
? |
3.3.2.6 | more |
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 |
? |
- |
? |
3.3.2.6 | more |
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 | more |
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 | more |
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 | more |
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 |
? |
- |
? |
3.3.2.6 | more |
the aminopeptidase binding site shares a similar structure to LTA4H at its ligand binding sites |
Homo sapiens |
? |
- |
? |
3.3.2.6 | more |
the aminopeptidase binding site shares a similar structure to LTA4H at its ligand binding sites |
Mus musculus |
? |
- |
? |
3.3.2.6 | L-arginine + H2O |
the best proteinogenic amino acid recognized by the enzyme is L-arginine |
Homo sapiens |
? |
- |
? |