CATH Classification

Domain Context

CATH Clusters

Superfamily Peptidase/esterase 'gauge' domain
Functional Family

Enzyme Information

3.4.19.1
Acylaminoacyl-peptidase.
based on mapping to UniProt Q9YBQ2
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
-!- 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.

UniProtKB Entries (1)

Q9YBQ2
APEH_AERPE
Aeropyrum pernix K1
Acylamino-acid-releasing enzyme

PDB Structure

PDB 2QR5
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase
Kiss, A.L., Pallo, A., Naray-Szabo, G., Harmat, V., Polgar, L.
J.Struct.Biol.