Acylpeptide hydrolase activity from erythrocytes.
Acylpeptide hydrolase, which cleaves the NH2-terminal acetylated or formylated amino acid from a blocked peptide, has been purified to apparent homogeneity from human erythrocytes. The enzyme catalyzes the hydrolysis of a diverse number of peptides and displays different pH optima for certain substrates in doing so. Zinc inhibits to the same extent the hydrolysis of both the most efficient and the least efficient substrates. This enzyme may play a pivotal role in the processing of polypeptide chains during biosynthesis.
D000409:Alanine / Q000031:analogs & derivatives / Q000097:blood; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000097:blood*; D055598:Chemical Phenomena; D002621:Chemistry; D004912:Erythrocytes / Q000201:enzymology*; D005971:Glutamates / Q000097:blood; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010447:Peptide Hydrolases / Q000097:blood*; D010455:Peptides / Q000097:blood; D013379:Substrate Specificity; D015032:Zinc / Q000494:pharmacology
D005971:Glutamates; D010455:Peptides; C044357:acetylalanine 4-nitroanilide; C044358:N-acetylglutamate 4-nitroanilide; D010447:Peptide Hydrolases; D000626:Aminopeptidases; C038220:acylaminoacyl-peptidase; D015032:Zinc; D000409:Alanine