Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 7, Pages 2080-2085Publisher
NATL ACAD SCIENCES
DOI: 10.1073/PNAS.0608876104
Keywords
enzymatic catalysis; Michaelis complex; solid-state NMR
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Funding
- NIGMS NIH HHS [GM49964] Funding Source: Medline
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0815865] Funding Source: National Science Foundation
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The highly efficient glycolytic enzyme, triosephosphate isomerase, is expected to differentially stabilize the proposed stable reaction species: ketone, aldehyde, and enediol(ate). The identity and steady-state populations of the chemical entities bound to triosephosphate isomerase have been probed by using solid- and solution-state NMR. The C-13-enriched ketone substrate, dihydroxyacetone phosphate, was bound to the enzyme and characterized at steady state over a range of sample conditions. The ketone substrate was observed to be the major species over a temperature range from -60 degrees C to 15 degrees C. Thus, there is no suggestion that the enzyme preferentially stabilizes the reactive intermediate or the product. The predominance of dihydroxyacetone phosphate on the enzyme would support a mechanism in which the initial proton abstraction in the reaction from clihydroxyacetone phosphate to D-glyceralclehyde 3-phosphate is significantly slower than the subsequent chemical steps.
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