Carboxypeptidase

spinqualitylabelsall models Pig carboxypeptidase B complex with acetate and Zn+2 ions (grey) (PDB code 3wc6) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Carboxypeptidase B (CPB) or thrombin activated fibrinolysis inhibitor or TAFIa cleaves preferentially positively charged amino acids. 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 carboxypeptidase (PCP) cleaves preferentially C termini amino acids preceded by proline. Tubulinyl-Tyr carboxypeptidase or vasohibin (TTCP) removes the C-terminal Tyr of tubulin. 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. See also Protease. Relevance Glutamate carboxypeptidase II is a potential target for imaging and therapy of prostate carcinoma and attenuation of neurotoxicity. Structural highlights The active site Zn+2 is located at the bottom of a pocket open to the surface of the enzyme. 3D Structures of Carboxypeptidase Carboxypeptidase 3D structures

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