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Science 24 March 1989:
Vol. 243. no. 4898, pp. 1591 - 1593
DOI: 10.1126/science.2928795
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Articles

Science, Vol 243, Issue 4898, 1591-1593
Copyright © 1989 by American Association for the Advancement of Science

articles

Major enhancement of the affinity of an enzyme for a transition-state analog by a single hydroxyl group

WM Kati and R Wolfenden

Department of Biochemistry, University of North Carolina, Chapel Hill 27514.

The compound 1,6-dihydropurine ribonucleoside, prepared by reduction of nebularine in the presence of ultraviolet light, is bound by adenosine deaminase approximately 10(8)-fold less tightly than 6-hydroxy-1,6-dihydropurine ribonucleoside, a nearly ideal transition-state analog. This difference in affinities, which is associated with the presence of a single hydroxyl group in the second compound, suggests the degree to which one or a few hydrogen bonds may stabilize the transition state in an enzyme reaction of this type.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
In Vivo Reshaping the Catalytic Site of Nucleoside 2'-Deoxyribosyltransferase for Dideoxy- and Didehydronucleosides via a Single Amino Acid Substitution.
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Improving Nucleoside Diphosphate Kinase for Antiviral Nucleotide Analogs Activation.
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Inhibition of Escherichia coli Glucosamine-6-phosphate Synthase by Reactive Intermediate Analogues. THE ROLE OF THE 2-AMINO FUNCTION IN CATALYSIS.
S. L. Bearne and C. Blouin (2000)
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   Abstract »    Full Text »    PDF »
Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.
D. Wilson, F. Rudolph, and F. Quiocho (1991)
Science 252, 1278-1284
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