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Literature summary extracted from
- Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos (2015), Int. J. Mol. Sci., 16, 6217-6234 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | drug development | enzyme APH is believed to be an important target for drug design | Aeropyrum pernix |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.19.1 | chlorpyrifosmethyl oxon | - |
Aeropyrum pernix |  |
| 3.4.19.1 | dichlorvos | - |
Aeropyrum pernix | |
| 3.4.19.1 | additional information | different organophosphorous compounds bind to the enzyme inducing conformational changes in two domains, namely, alpha/beta hydrolase and beta-propeller, computational study of APH bound to chlorpyrifosmethyl oxon and dichlorvos, and molecular dynamics simulations of enzyme bound to the inhibitors, the starting model of APH is derived from 2.7 A resolution crystal structure of acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (PDB ID 1VE7), overview. The docking study reveals that Val471 and Gly368 are important residues for chlorpyrifosmethyl oxon and dichlorvos binding | Aeropyrum pernix |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.19.1 | additional information | - |
additional information | thermodynamics | Aeropyrum pernix |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.19.1 | Aeropyrum pernix | Q9YBQ2 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.19.1 | additional information | enzyme APH catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids | Aeropyrum pernix | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | acylpeptide hydrolase | - |
Aeropyrum pernix |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.19.1 | evolution | the enzyme belongs to the prolyl oligopeptidase family of serine proteases | Aeropyrum pernix |
| 3.4.19.1 | physiological function | acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides | Aeropyrum pernix |
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Release 2023.1 (January 2023)
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