STEREOCHEMICAL ANALYSIS OF THE SPECIFICITY OF PANCREATIC RNASE WITH POLYFORMYCIN AS SUBSTRATE: DIFFERENTIATION OF THE TRANSPHOSPHORYLATION AND HYDROLYSIS REACTIONS*

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RESUMO

A stereochemical analysis of the substrate and inhibitor specificities of bovine pancreatic ribonuclease A is presented. A scheme is proposed in which the binding specificity for this protein-nucleic acid interaction is rationalized in terms of a simple system of H-bonds. The functional groups that govern substrate binding for transphosphorylation and hydrolysis, respectively, are considered and differentiated, and predictions are offered concerning the interaction of presumptive substrates with RNase.

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