Carboxypeptidase

Function

Carboxypeptidase (CP) cleaves the amino acid at the C terminal of a polypeptide chain. 2-guanidinoethylmercaptosuccinic acid (GEMSA) is a potent inhibitor of CP.

• Carboxypeptidase A (CPA) cleaves preferentially aromatic or branched-chain amino acids.^[1]
  
• Carboxypeptidase B (CPB) cleaves preferentially positively charged amino acids.^[2]
  
• Carboxypeptidase D (CPD) cleaves preferentially Arg or Lys at the C-terminal.
  
• Carboxypeptidase E (CPE) cleaves preferentially Arg or Lys at the C-terminal.
  
• Carboxypeptidase M (CPM) is membrane-bound and cleaves preferentially Arg or Lys.
  
• Carboxypeptidase N (CPN) is a plasma Zn metalloprotease which cleaves preferentially Arg or Lys at the C-terminal.
  
• Carboxypeptidase T (CPT) cleaves preferentially Arg, Lys or hydrophobic residues at the C-terminal.
  
• Carboxypeptidase Y (CPY) is a yeast protease which cleaves at the C-terminal.
  
• Carboxypeptidase M32 is a Zn containing metalloprotease.
  
• Glutamate carboxypeptidase (GCP) cleaves glutamate from the peptide N-acetyl-aspartyl-glutamate.
  
• Prolyl arboxypeptidase (PCP) cleaves preferentially C termini amino acids preceded by proline.
  
• D-alanyl-D-alanine carboxypeptidase (AACP) cross-links peptidoglycan chains is also PBP.
  
• Procarboxypeptidases are zymogens which undergo cleavage in order to become an active carboxypeptidase.

Relevance

Glutamate carboxypeptidase II is a potential target for imaging and therapy of prostate carcinoma and attenuation of neurotoxicity.

Structural highlights

The is located at the bottom of a pocket open to the surface of the enzyme.^[3]