Stereochemistry in inactivation of carboxypeptidase A. structural analysis of the inactivated carboxypeptidase a by an enantiomeric pair of 2-benzyl-3, 4-epoxybutanoic acids

摘要

The X-ray crystal structure of inactivated carboxypeptidase a by (2R, 3S)-2-benzyl-3 4-epoxybutanoic acid, a pseudomechanism-based inactivator, was determined to show that the carboxylate of Glu-270 at the active site of the enzyme is covalently modified: the inhibitor is tethered to the carboxylate forming an ester linkage which is brought about by the attack of the carboxylate on the oxirane ring of the inhibitor.