The structures of the transition states for a variety of enzyme-catalyzed ribosyl group transfer reactions, determined by computational evaluation of multiple tritium and heavy atom kinetic isotope effects on these enzymatic reactions, have been found to show a considerable variation in the extent of bond cleavage at the ribosyl anomeric carbon. The calculated transition-state structures have been used to guide the design of high-affinity transition-state analogue inhibitors for 5'-methylthioadenosine nucleosidases with potential as therapeutic agents.
Rational design of transition-state analogues as potent enzyme inhibitors with therapeutic applications. Publishing Authors By Initials
Rational design of transition-state analogues as potent enzyme inhibitors with therapeutic applications. Journal Published:
PUBLICATION TYPE: Review
Journal: ACS chemical biology
VOLUME: 2
Page Numbers: 711-4
Journal Abbreviation: ACS Chem. Biol.
ISSN: 1554-8937
DAY: 20
MONTH: Nov
YEAR: 2007
Rational design of transition-state analogues as potent enzyme inhibitors with therapeutic applications. Information
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LANGUAGE: eng
NlmUniqueID: 101282906
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Grant and Affiliation Information for Rational design of transition-state analogues as potent enzyme inhibitors with therapeutic applications.
AFFILIATION: Department of Chemistry, University at Buffalo, State University of New York, Buffalo, New York 14260-3000, USA.
Country: United States
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MEDLINETA: ACS Chem Biol
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