Carboxypeptidase

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Contents

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) or thrombin activated fibrinolysis inhibitor or TAFIa 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 carboxypeptidase (PCP) cleaves preferentially C termini amino acids preceded by proline.
  • Tubulinyl-Tyr carboxypeptidase or vasohibin (TTCP) removes the C-terminal Tyr of tubulin[3].
  • 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.[4]

3D Structures of Carboxypeptidase

Carboxypeptidase 3D structures


Pig carboxypeptidase B complex with acetate and Zn+2 ions (grey) (PDB code 3wc6)

Drag the structure with the mouse to rotate


References

  1. ↑ Fernandez D, Boix E, Pallares I, Aviles FX, Vendrell J. Structural and Functional Analysis of the Complex between Citrate and the Zinc Peptidase Carboxypeptidase A. Enzyme Res. 2011;2011:128676. doi: 10.4061/2011/128676. Epub 2011 Jul 25. PMID:21804935 doi:10.4061/2011/128676
  2. ↑ Adler M, Bryant J, Buckman B, Islam I, Larsen B, Finster S, Kent L, May K, Mohan R, Yuan S, Whitlow M. Crystal structures of potent thiol-based inhibitors bound to carboxypeptidase B. Biochemistry. 2005 Jul 5;44(26):9339-47. PMID:15982000 doi:http://dx.doi.org/10.1021/bi0501941
  3. ↑ Arce CA, Barra HS. Association of tubulinyl-tyrosine carboxypeptidase with microtubules. FEBS Lett. 1983 Jun 27;157(1):75-8. doi: 10.1016/0014-5793(83)81119-3. PMID:6862022 doi:http://dx.doi.org/10.1016/0014-5793(83)81119-3
  4. ↑ Yoshimoto N, Itoh T, Inaba Y, Ishii H, Yamamoto K. Structural Basis for Inhibition of Carboxypeptidase B by Selenium-Containing Inhibitor: Selenium Coordinates to Zinc in Enzyme. J Med Chem. 2013 Sep 24. PMID:24010887 doi:10.1021/jm400816v

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