Carboxypeptidase

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'''Carboxypeptidase''' (CP) cleaves the amino acid at the C terminal of a polypeptide chain. 2-guanidinoethylmercaptosuccinic acid (GEMSA) is a potent inhibitor of CP.<br />
'''Carboxypeptidase''' (CP) cleaves the amino acid at the C terminal of a polypeptide chain. 2-guanidinoethylmercaptosuccinic acid (GEMSA) is a potent inhibitor of CP.<br />
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* '''[[Carboxypeptidase_A|Carboxypeptidase A]]''' (CPA) cleaves preferentially aromatic or branched-chain amino acids.<ref>PMID:21804935</ref><br /> For detatils see [[Carboxypeptidase A]].
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* '''[[Carboxypeptidase_A|Carboxypeptidase A]]''' (CPA) cleaves preferentially aromatic or branched-chain amino acids.<ref>PMID:21804935</ref><br />
* '''Carboxypeptidase B''' (CPB) cleaves preferentially positively charged amino acids.<ref>PMID:15982000</ref><br />
* '''Carboxypeptidase B''' (CPB) cleaves preferentially positively charged amino acids.<ref>PMID:15982000</ref><br />
* '''Carboxypeptidase D''' (CPD) cleaves preferentially Arg or Lys at the C-terminal.<br />
* '''Carboxypeptidase D''' (CPD) cleaves preferentially Arg or Lys at the C-terminal.<br />

Revision as of 10:47, 18 December 2019

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

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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. 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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