EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
   3.4.19.1 | 2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O |
endopeptidase activity |
Aeropyrum pernix |
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala |
- |
? |
| 3.4.19.1 | 4-nitrophenyl caprylate + H2O |
- |
Aeropyrum pernix |
4-nitrophenol + caprylate |
- |
? |
| 3.4.19.1 | Ac-Ala-Ala + H2O |
- |
Aeropyrum pernix |
Ac-Ala + Ala |
- |
? |
| 3.4.19.1 | Ac-Ala-Ala-Ala + H2O |
- |
Aeropyrum pernix |
Ac-Ala + Ala-Ala |
- |
? |
| 3.4.19.1 | Ac-Ala-Ala-Ala-Ala + H2O |
- |
Aeropyrum pernix |
Ac-Ala + Ala-Ala-Ala |
- |
? |
| 3.4.19.1 | Ac-Leu-4-nitroanilide + H2O |
- |
Aeropyrum pernix |
Ac-Leu + 4-nitroaniline |
- |
? |
| 3.4.19.1 | acetyl-Phe-2-naphthylamide + H2O |
- |
Aeropyrum pernix |
acetyl-Phe + 2-naphthylamine |
- |
? |
| 3.4.19.1 | more |
hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble |
Aeropyrum pernix |
? |
- |
? |
| 3.4.19.1 | more |
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments |
Aeropyrum pernix |
? |
- |
? |
| 3.4.19.1 | more |
enzyme APH catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids |
Aeropyrum pernix |
? |
- |
? |
