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ENZYME entry: EC 3.4.19.1

Accepted Name
Acylaminoacyl-peptidase.
Alternative Name(s)
Acylamino-acid-releasing enzyme.
N-acylpeptide hydrolase.
Reaction catalysed
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
Comment(s)
  • Best if P1 = Ser, Ala, Met; poor if P1 = Gly, Tyr, Asp, Asn or Pro.
  • Group of similar enzymes liberating N-acetyl or N-formyl amino acid from proteins and peptides.
  • Active at neutral pH.
  • Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides.
  • Display dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of misrecognition of the glycyl residue as an uncharged N-acyl group.
  • Inhibited by diisopropyl fluorophosphate.
  • Belongs to peptidase family S9C.
  • Formerly EC 3.4.14.3.
Cross-references
PROSITEPDOC00587
BRENDA3.4.19.1
EC2PDB3.4.19.1
ExplorEnz3.4.19.1
PRIAM enzyme-specific profiles3.4.19.1
KEGG Ligand Database for Enzyme Nomenclature3.4.19.1
IUBMB Enzyme Nomenclature3.4.19.1
IntEnz3.4.19.1
MEDLINEFind literature relating to 3.4.19.1
MetaCyc3.4.19.1
UniProtKB/Swiss-Prot
Q0IXP9, AARE1_ORYSJ;  Q338C0, AARE2_ORYSJ;  Q84LM4, AARE_ARATH;  
P80227, ACPH_BOVIN;  P13798, ACPH_HUMAN;  P19205, ACPH_PIG;  
P25154, ACPH_RABIT;  P13676, ACPH_RAT;  Q9YBQ2, APEH_AERPE;  
Q8R146, APEH_MOUSE;  

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