Transition-state characterization: a new approach combining inhibitor analogs and variation in enzyme structure

A new strategy of potentially broad application for probing transition-state (TS) analogy in enzymatic systems is described in this paper. The degree to which a series of phosphonate inhibitors act as TS analogues of rat carboxypeptidase A1 has been determined for the wild-type enzyme, for the R127K...

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Veröffentlicht in:	Biochemistry (Easton) 1992-02, Vol.31 (4), p.959-963
Hauptverfasser:	Phillips, Margaret A, Kaplan, Alan P, Rutter, William J, Bartlett, Paul A
Format:	Artikel
Sprache:	eng
Schlagworte:	analogs Analytical, structural and metabolic biochemistry Animals Biological and medical sciences carboxypeptidase A1 Carboxypeptidases - antagonists & inhibitors Carboxypeptidases - chemistry Carboxypeptidases - genetics Carboxypeptidases A Catalysis Dipeptides - chemistry Dipeptides - pharmacology Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology General aspects, investigation methods Genetic Variation Guanidine Guanidines - chemistry Hydrolysis inhibition Kinetics Mutation Organophosphonates - chemistry Organophosphonates - pharmacology phosphonic acid Rats Structure-Activity Relationship Substrate Specificity
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