EC 3.4.19.1 - Acylaminoacyl-peptidase

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IntEnz Enzyme Nomenclature
EC 3.4.19.1

Names

Accepted name:
acylaminoacyl-peptidase
Other names:
N-acylpeptide hydrolase
N-formylmethionine (fMet) aminopeptidase
α-N-acylpeptide hydrolase
acylamino-acid-releasing enzyme
Systematic name:
-

Reaction

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). Formerly EC 3.4.14.3.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00587
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004254
CAS Registry Number: 73562-30-8
UniProtKB/Swiss-Prot: (10) [show] [UniProt]

References

  1. Tsunazawa, S., Narita, K. and Ogata, K.
    Acylamino acid-releasing enzyme from rat liver.
    J. Biochem. 77: 89-102 (1975). [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: 205-211 (1979). [PMID: 477668]
  3. Kobayashi, K. and Smith, J.A.
    Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction.
    J. Biol. Chem. 262: 11435-11437 (1987). [PMID: 3305492]

[EC 3.4.19.1 created 1978 as EC 3.4.14.3, transferred 1981 to EC 3.4.19.1]