Application | Comment | Organism |
---|---|---|
drug development | enzyme APH is believed to be an important target for drug design | Aeropyrum pernix |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
chlorpyrifosmethyl oxon | - |
Aeropyrum pernix | |
dichlorvos | - |
Aeropyrum pernix | |
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | thermodynamics | Aeropyrum pernix |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aeropyrum pernix | Q9YBQ2 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | enzyme APH catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids | Aeropyrum pernix | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
acylpeptide hydrolase | - |
Aeropyrum pernix |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the prolyl oligopeptidase family of serine proteases | Aeropyrum pernix |
physiological function | acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides | Aeropyrum pernix |