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carboxypeptidase A2 (CPA2)
Function:
- release of a C-terminal amino acid
- preference for bulkier C-terminal residues
Cofactor: binds 1 Zn+2 ion per subunit
Structure: belongs to the peptidase M14 family
Compartment: secreted
General
carboxypeptidase-A
Properties
SIZE: entity length = 417 aa
MW = 47 kD
COMPARTMENT: extracellular compartment
MOTIF: signal sequence {1-16}
Substrate binding {177-180}
MOTIF: Zn+2-binding site
SITE: 177-177
Zn+2-binding site
SITE: 180-180
binding site
SITE: 235-235
FOR-BINDING-OF: Substrate
cysteine residue {C246}
MODIFICATION: cysteine residue {C269}
Substrate binding {252-253}
cysteine residue {C269}
MODIFICATION: cysteine residue {C246}
Zn+2-binding site
SITE: 304-304
Substrate binding {305-306}
cysteine residue {C318}
MODIFICATION: cysteine residue {C352}
cysteine residue {C352}
MODIFICATION: cysteine residue {C318}
glutamate residue {E378}
Database Correlations
OMIM 600688
UniProt P48052
PFAM correlations
Entrez Gene 1358
ENZYME 3.4.17.15
References
UniProt :accession P48052