Detection of an anhydride intermediate in the carboxypeptidase A catalyzed hydrolysis of a peptide substrate by solid state NMR spectroscopy and its mechanistic implication

Bioorg Med Chem Lett. 1998 Dec 1;8(23):3379-84. doi: 10.1016/s0960-894x(98)00624-6.

Abstract

We have detected an anhydride intermediate in the CPA catalyzed proteolytic reaction of Gly-Tyr. It appears that since the zinc-bound water molecule which is believed to attack the scissile amide carbonyl carbon in the hydrolysis reaction is excluded by the N-terminal amino group of Gly-Tyr, the carboxylate of Glu-270 becomes to attack the amide bond to generate the anhydride intermediate.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anhydrides / analysis*
  • Carboxypeptidases / metabolism*
  • Carboxypeptidases A
  • Catalysis
  • Dipeptides / metabolism*
  • Hydrolysis
  • Magnetic Resonance Spectroscopy

Substances

  • Anhydrides
  • Dipeptides
  • glycyltyrosine
  • Carboxypeptidases
  • Carboxypeptidases A