[Theoretical conformational analysis of a substrate component of tetrahedral intermediates and of acyl-enzyme of carboxypeptidase A].
Semi-empirical calculation of conformational properties of covalent complexes of carboxypeptidase A with ester and peptide substrates are presented. There is a favourable form of transient tetrahedral and covalent acyl-enzyme intermediates in the active site of carboxypeptidase A. The ester and peptide substrates bind in the active site of carbopeptidase A in the same mode. The transition from one stage of the reaction to the other is followed by a small conformational change. The atom coordinates of the substrate component of these complexes are presented.
D001665:Binding Sites; D002268:Carboxypeptidases / Q000378:metabolism*; D043422:Carboxypeptidases A; D006868:Hydrolysis; D007700:Kinetics; D010455:Peptides; D011485:Protein Binding; D011487:Protein Conformation
D010455:Peptides; D002268:Carboxypeptidases; D043422:Carboxypeptidases A
Teoreticheskiĭ konformatsionnyĭ analiz substratnykh komponentov tetraédricheskikh adduktov i atsilfermenta karboksipeptidazy A.