title: Detection of an anhydride intermediate in the carboxypeptidase A catalyzed hydrolysis of a peptide substrate by solid state NMR spectroscopy and its mechanistic implication.
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.
authors.affiliation: Department of Chemistry, Pohang University of Science and Technology, Korea.
authors.forename: H C
authors.initials: HC
authors.lastname: Lee
authors.forename: Y H
authors.initials: YH
authors.lastname: Ko
authors.forename: S B
authors.initials: SB
authors.lastname: Baek
authors.forename: D H
authors.initials: DH
authors.lastname: Kim
mesh_terms: D000812:Anhydrides / Q000032:analysis*; D002268:Carboxypeptidases / Q000378:metabolism*; D043422:Carboxypeptidases A; D002384:Catalysis; D004151:Dipeptides / Q000378:metabolism*; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy
chemical_list: D000812:Anhydrides; D004151:Dipeptides; C022013:glycyltyrosine; D002268:Carboxypeptidases; D043422:Carboxypeptidases A