Major Enhancement of the Affinity of an Enzyme for a Transition-State Analog by a Single Hydroxyl Group
- 24 March 1989
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 243 (4898) , 1591-1593
- https://doi.org/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.Keywords
This publication has 21 references indexed in Scilit:
- Transition-state stabilization by adenosine deaminase: 1,6-addition of water to purine ribonucleoside, the enzyme's affinity for 6-hydroxy-1,6-dihydropurine ribonucleoside, and the effective concentration of substrate water at the active siteBiochemistry, 1989
- Preliminary X-ray analysis of crystals of murine adenosine deaminaseJournal of Molecular Biology, 1988
- Adenosine deaminase converts purine riboside into an analog of a reactive intermediate: a carbon-13 NMR and kinetic studyBiochemistry, 1987
- How rare are the covalent hydrates of purine ribonucleoside and nicotinamide? A method for estimating positions of highly unfavorable equilibriaJournal of the American Chemical Society, 1986
- Transition-state stabilization by adenosine deaminase: structural studies of its inhibitory complex with deoxycoformycinBiochemistry, 1986
- Adenosine deaminase: solvent isotope and pH effects on the binding of transition-state and ground-state analog inhibitorsBiochemistry, 1983
- The absolute stereochemistry of nebularine-methanol photoadduct. A potential transition-state analog of adenosine deaminase.CHEMICAL & PHARMACEUTICAL BULLETIN, 1983
- Hydratase activity of a hydrolase. Adenosine deaminaseJournal of the American Chemical Society, 1972
- Ring-modified substrates of adenosine deaminasesBiochemistry, 1969
- The energy and entropy of hydration of organic compoundsTransactions of the Faraday Society, 1937