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Use of isotope effects to determine enzyme mechanisms

✍ Scribed by W. W. Cleland

Publisher
John Wiley and Sons
Year
2007
Tongue
French
Weight
159 KB
Volume
50
Category
Article
ISSN
0022-2135

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✦ Synopsis

Abstract

Isotope effects are a powerful tool for determining the mechanisms of enzymatic reactions. Methods for measurement of isotope effects are reviewed and the equations that describe observed isotope effects and permit determination of intrinsic isotope effects on the isotope‐sensitive step are presented. Aspartate transcarbamoylase is used as an example for how the kinetic mechanism can be determined by observing the size of an isotope effect as a function of the concentration of another substrate. Cytidine, adenosine and AMP deaminases are used to illustrate determining the relative rates of steps in the mechanism. Determination of chemical mechanism is illustrated by data for malic enzyme, OMP decarboxylase, aspartate transcarbamoylase, L‐ribulose‐5‐P 4‐epimerase, oxalate decarboxylase, tryptophan 2‐monooxygenase and the K58A mutant of aspartate aminotransferase when rescued by ammonia. Determination of transition state structure is illustrated by data for formate dehydrogenase, prephenate dehydrogenase, chorismate mutase, as well as for enzymes that catalyze phosphoryl and acyl transfer. Copyright © 2007 John Wiley & Sons, Ltd.

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