EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   3.3.2.6 | more |
LTA4H is a zinc metalloprotease |
Rattus norvegicus |
? |
- |
? |
| 3.3.2.6 | more |
LTA4H is a zinc metalloprotease |
Canis lupus familiaris |
? |
- |
? |
| 3.3.2.6 | more |
no activity with L-Asn, L-Asp, L-Glu, Gly, L-Ile, L-Thr, L-Trp, L-Val, as well as D-amino acids |
Homo sapiens |
? |
- |
? |
| 3.3.2.6 | more |
proline-glycine-proline (PGP) is a substrate for the enzyme's aminopeptidase (AP) activity |
Rattus norvegicus |
? |
- |
? |
| 3.3.2.6 | more |
proline-glycine-proline (PGP) is a substrate for the enzyme's aminopeptidase (AP) activity |
Homo sapiens |
? |
- |
? |
| 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 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 | proline-4-nitroanilide + H2O |
- |
Homo sapiens |
proline + 4-nitroaniline |
- |
? |
| 3.3.2.6 | proline-glycine-proline + H2O |
PGP |
Homo sapiens |
? |
- |
? |
