ArticleJournal of the American Chemical Society2014
Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 35 citations in OpenAlex.
- The Role of Protein Side Chains in Enzyme-Activating Conformational Changes: Lessons from Studies on Variant Enzymes.Chemical reviews · 2025Review
- Enzyme Architecture: Activation of Phosphite Dehydrogenase-Catalyzed Hydride Transfer by NADBiochemistry · 2025Article
- Glycerol 3-Phosphate Dehydrogenase Catalyzed Hydride Transfer: Enzyme Activation by Cofactor Pieces.Biochemistry · 2024Article
- Utilization of Cofactor Binding Energy for Enzyme Catalysis: Formate Dehydrogenase-Catalyzed Reactions of the Whole NAD Cofactor and Cofactor Pieces.Biochemistry · 2023Article
- The Role of Asn11 in Catalysis by Triosephosphate Isomerase.Biochemistry · 2023Article
- Kinetics and mechanism for enzyme-catalyzed reactions of substrate pieces.Methods in enzymology · 2023Article
- Adenylate Kinase-Catalyzed Reactions of AMP in Pieces: Specificity for Catalysis at the Nucleoside Activator and Dianion Catalytic Sites.Biochemistry · 2022Article
- Enabling Role of Ligand-Driven Conformational Changes in Enzyme Evolution.Biochemistry · 2022Review
- Protein-Ribofuranosyl Interactions Activate Orotidine 5'-Monophosphate Decarboxylase for Catalysis.Biochemistry · 2021Article
- Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe.Accounts of chemical research · 2021Review
- Phosphodianion Activation of Enzymes for Catalysis of Central Metabolic Reactions.Journal of the American Chemical Society · 2021Article
- The role of ligand-gated conformational changes in enzyme catalysis.Biochemical Society transactions · 2019Review
- Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis.Journal of the American Chemical Society · 2019Article
- Human Glycerol 3-Phosphate Dehydrogenase: X-ray Crystal Structures That Guide the Interpretation of Mutagenesis Studies.Biochemistry · 2019Article
- Enzyme Architecture: Breaking Down the Catalytic Cage that Activates Orotidine 5'-Monophosphate Decarboxylase for Catalysis.Journal of the American Chemical Society · 2018Article
- Primary Deuterium Kinetic Isotope Effects: A Probe for the Origin of the Rate Acceleration for Hydride Transfer Catalyzed by Glycerol-3-Phosphate Dehydrogenase.Biochemistry · 2018Article
- Enzyme Architecture: Amino Acid Side-Chains That Function To Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase.Journal of the American Chemical Society · 2018Article
- Enzyme Architecture: The Role of a Flexible Loop in Activation of Glycerol-3-phosphate Dehydrogenase for Catalysis of Hydride Transfer.Biochemistry · 2018Article
- Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase.Journal of the American Chemical Society · 2018Article
- A reevaluation of the origin of the rate acceleration for enzyme-catalyzed hydride transfer.Organic & biomolecular chemistry · 2017Review
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3 authors at 1 institution in 1 country.
Funding
Abstract
Values of (k(cat)/K(m))GAP for triosephosphate isomerase-catalyzed reactions of (R)-glyceraldehyde 3-phosphate and k(cat)/K(HPi)K(GA) for reactions of the substrate pieces glycolaldehyde and HPO3(2-) have been determined for wild-type and the following TIM mutants: I172V, I172A, L232A, and P168A (TIM from Trypanosoma brucei brucei); a 208-TGAG for 208-YGGS loop 7 replacement mutant (L7RM, TIM from chicken muscle); and, Y208T, Y208S, Y208A, Y208F and S211A (yeast TIM). A superb linear logarithmic correlation, with slope of 1.04 ± 0.03, is observed between the kinetic parameters for wild-type and most mutant enzymes, with positive deviations for L232A and L7RM. The unit slope shows that most mutations result in an identical change in the activation barriers for the catalyzed reactions of whole substrate and substrate pieces, so that the two transition states are stabilized by similar interactions with the protein catalyst. This is consistent with a role for dianions as active spectators, which hold TIM in a catalytically active caged form.
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