Open AccessSTEREOCHEMICAL ANALYSIS OF THE SPECIFICITY OF PANCREATIC RNASE WITH POLYFORMYCIN AS SUBSTRATE: DIFFERENTIATION OF THE TRANSPHOSPHORYLATION AND HYDROLYSIS REACTIONS
Author(s) -
David C. Ward,
W. Fuller,
E. Reich
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.62.2.581
Subject(s) - bovine pancreatic ribonuclease , rnase p , pancreatic ribonuclease , substrate (aquarium) , ribonuclease , chemistry , hydrolysis , nucleic acid , rnase h , stereochemistry , enzyme , biochemistry , rna , biology , ecology , gene
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.