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Literature summary for 3.4.19.1 extracted from

  • Jin, H.; Zhou, Z.; Wang, D.; Guan, S.; Han, W.
    Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos (2015), Int. J. Mol. Sci., 16, 6217-6234 .
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
drug development enzyme APH is believed to be an important target for drug design Aeropyrum pernix

Inhibitors

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 [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamics Aeropyrum pernix

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
acylpeptide hydrolase
-
Aeropyrum pernix

General Information

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