| EC |
3.4.19.1 |
| Accepted name: |
acylaminoacyl-peptidase |
| Reaction: |
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide |
| Other name(s): |
acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase |
| Comments: |
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). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 73562-30-8 |
| References: |
| 1. |
Tsunazawa, S., Narita, K. and Ogata, K. Acylamino acid-releasing enzyme from rat liver. J. Biochem. (Tokyo) 77 (1975) 89–102. [PMID: 1137989] |
| 2. |
Ungar, T., Nagelschmidt, M. and Struck, H. N-Acetylaminoacyl-p-nitranilidase from human placenta. Purification and some properties. Eur. J. Biochem. 97 (1979) 205–211. [DOI] [PMID: 477668] |
| 3. |
Kobayashi, K. and Smith, J.A. Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction. J. Biol. Chem. 262 (1987) 11435–11437. [PMID: 3305492] |
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| [EC 3.4.19.1 created 1978 as EC 3.4.14.3, transferred 1981 to EC 3.4.19.1] |
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