EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
   3.4.19.1 | more |
the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview |
Aeropyrum pernix |
? |
- |
? |
| 3.4.19.1 | more |
the enzyme is also active with fatty acid esters, e.g. with 4-nitrophenyl caprylate. Substrate binding mechanism analysis, and random acceleration and steered molecular dynamics simulations of ligands unbinding pathways from APH. Three main pathways are observed most frequently, namely P1, P2A, and P3, evaluation by comparing the average force profiles and potential of mean force calculations revealing that P3 is the unbinding pathway. Overview |
Aeropyrum pernix |
? |
- |
? |
| 3.4.19.1 | N-acetyl-L-Leu-4-nitroanilide + H2O |
- |
Aeropyrum pernix |
N-acetyl-L-Leu + 4-nitroaniline |
- |
? |
| 3.4.19.1 | N-acetyl-Leu-4-nitroanilide + H2O |
switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase |
Aeropyrum pernix |
N-acetyl-L-Leu + 4-nitroaniline |
- |
? |
| 3.4.19.1 | N-acetyl-Leu-p-nitroanilide + H2O |
esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished |
Aeropyrum pernix |
N-acetyl-Leu + p-nitroaniline |
- |
? |
| 3.4.19.1 | N-acetyl-Phe-2-naphthylamide + H2O |
- |
Aeropyrum pernix |
N-acetyl-Phe + 2-naphthylamine |
- |
? |
| 3.4.19.1 | p-nitrophenyl caprylate + H2O |
esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished |
Aeropyrum pernix |
nitrophenol + caprylate |
- |
? |
| 3.4.19.1 | 4-nitrophenyl caprylate + H2O |
- |
Aeropyrum pernix ATCC 700893 |
4-nitrophenol + caprylate |
- |
? |
| 3.4.19.1 | Ac-Ala-Ala + H2O |
- |
Aeropyrum pernix ATCC 700893 |
Ac-Ala + Ala |
- |
? |
| 3.4.19.1 | Ac-Ala-Ala-Ala + H2O |
- |
Aeropyrum pernix ATCC 700893 |
Ac-Ala + Ala-Ala |
- |
? |
