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Information on EC 3.4.19.1 - acylaminoacyl-peptidase

for references in articles please use BRENDA:EC3.4.19.1

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IUBMB 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).

The enzyme appears in viruses and cellular organisms
Reaction Schemes
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide

Synonyms
apaap, acylpeptide hydrolase, acylaminoacyl peptidase, acylamino acid-releasing enzyme, acyl-peptide hydrolase, spaap, aphdr, acyl peptide hydrolase, apaph, aare/oph, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
MetaCyc
Arg/N-end rule pathway (eukaryotic)