EC 188.8.131.52 - Acylaminoacyl-peptidase
IntEnz Enzyme Nomenclature
N-formylmethionine (fMet) aminopeptidase
- Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family S9 (prolyl oligopeptidase family). Formerly EC 184.108.40.206.
Links to other databases
Acylamino acid-releasing enzyme from rat liver.J. Biochem. 77: 89-102 (1975). [PMID: 1137989]
N-Acetylaminoacyl-p-nitranilidase from human placenta. Purification and some properties.Eur. J. Biochem. 97: 205-211 (1979). [PMID: 477668]
Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction.J. Biol. Chem. 262: 11435-11437 (1987). [PMID: 3305492]
[EC 220.127.116.11 created 1978 as EC 18.104.22.168, transferred 1981 to EC 22.214.171.124]