Reports

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

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Science  24 Mar 1989:
Vol. 243, Issue 4898, pp. 1591-1593
DOI: 10.1126/science.2928795

Abstract

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.

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