Hydride Transfer Catalyzed by Glycerol Phosphate Dehydrogenase: Recruitment of an Acidic Amino Acid Side Chain to Rescue a Damaged Enzyme
Author:
Affiliation:
1. Department of Chemistry, University at Buffalo, The State University of New York at Buffalo, Buffalo, New York 14260-3000, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00801
Reference30 articles.
1. Structural Studies on Nicotinamide Adenine Dinucleotide-linked l-Glycerol 3-Phosphate Dehydrogenase Crystallized from Rat Skeletal Muscle
2. A Substrate in Pieces: Allosteric Activation of Glycerol 3-Phosphate Dehydrogenase (NAD+) by Phosphite Dianion
3. Crystal Structures of Human Glycerol 3-phosphate Dehydrogenase 1 (GPD1)
4. Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis
5. Human Glycerol 3-Phosphate Dehydrogenase: X-ray Crystal Structures That Guide the Interpretation of Mutagenesis Studies
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2. Glycerol 3-Phosphate Dehydrogenase: Role of the Protein Conformational Change in Activation of a Readily Reversible Enzyme-Catalyzed Hydride Transfer Reaction;Biochemistry;2024-03-28
3. Adenylate Kinase-Catalyzed Reactions of AMP in Pieces: Specificity for Catalysis at the Nucleoside Activator and Dianion Catalytic Sites;Biochemistry;2022-11-22
4. Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis;Journal of Hematology & Oncology;2022-07-14
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