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ENZYME

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
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
Rhea expert-curated reactions3.4.19.1
UniProtKB/Swiss-Prot
Q0IXP9, AARE1_ORYSJQ338C0, AARE2_ORYSJQ84LM4, AARE_ARATH
P80227, ACPH_BOVINP13798, ACPH_HUMANQ8R146, ACPH_MOUSE
P19205, ACPH_PIGP25154, ACPH_RABITP13676, ACPH_RAT
Q9YBQ2, APEH_AERPE

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