STEREOCHEMICAL ANALYSIS OF THE SPECIFICITY OF PANCREATIC RNASE WITH POLYFORMYCIN AS SUBSTRATE: DIFFERENTIATION OF THE TRANSPHOSPHORYLATION AND HYDROLYSIS REACTIONS*
AUTOR(ES)
Ward, D. C.
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=277847Documentos Relacionados
- Stereochemical selectivity of group II intron splicing, reverse splicing, and hydrolysis reactions.
- SIMILARITY BETWEEN PHYSICOCHEMICAL AND BIOLOGICAL REACTIONS*
- Phosphate-Mediated Alteration of the Microsporum gypseum Germination Protease Specificity for Substrate: Enhanced Keratinase Activity
- Substrate specificity and kinetic framework of a DNAzyme with an expanded chemical repertoire: a putative RNaseA mimic that catalyzes RNA hydrolysis independent of a divalent metal cation
- Altering the Substrate Specificity of Organophosphorus Hydrolase for Enhanced Hydrolysis of Chlorpyrifos