Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions
Author:
Affiliation:
1. Department of Chemistry, University at Buffalo, SUNY, Buffalo, New York 14260-3000, United States
2. Department of Chemistry, Illinois State University, Normal, Illinois 61790-4160, 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.0c13423
Reference34 articles.
1. Binding Energy, Specificity, and Enzymic Catalysis: The Circe Effect
2. Enzymatic Catalysis of Proton Transfer at Carbon: Activation of Triosephosphate Isomerase by Phosphite Dianion
3. Hydron Transfer Catalyzed by Triosephosphate Isomerase. Products of the Direct and Phosphite-Activated Isomerization of [1-13C]-Glycolaldehyde in D2O
4. Contribution of Phosphate Intrinsic Binding Energy to the Enzymatic Rate Acceleration for Triosephosphate Isomerase
5. A Substrate in Pieces: Allosteric Activation of Glycerol 3-Phosphate Dehydrogenase (NAD+) by Phosphite Dianion
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