Structure–Reactivity Effects on Intrinsic Primary Kinetic Isotope Effects for Hydride Transfer Catalyzed by Glycerol-3-phosphate Dehydrogenase
Author:
Affiliation:
1. Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
http://pubs.acs.org/doi/pdf/10.1021/jacs.6b07028
Reference29 articles.
1. The Use of Isotope Effects to Determine Enzyme Mechanisms
2. Perfection in enzyme catalysis: the energetics of triosephosphate isomerase
3. Horse liver alcohol dehydrogenase SS: Purification and characterization of the homogeneous isoenzyme
4. Substrate concentration dependence of deuterium isotope effects on beef heart lactate dehydrogenase
5. Catalytic mechanism of Zn2+-dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu154→Cys forms of yeast xylitol dehydrogenase
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