ArticleBiochemistry2013
Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 32 citations in OpenAlex.
- Mechanistic and Molecular Dynamics Studies Reveal that Increased Loop 3 Mobility Alters Substrate Capture in an NADH:Quinone Oxidoreductase.Biochemistry · 2026Article
- The Role of Protein Side Chains in Enzyme-Activating Conformational Changes: Lessons from Studies on Variant Enzymes.Chemical reviews · 2025Review
- Ribosome External Electric Field Regulates Metabolic Enzyme Activity: The RAMBO Effect.The journal of physical chemistry. B · 2024Article
- Triosephosphate Isomerase: The Crippling Effect of the P168A/I172A Substitution at the Heart of an Enzyme Active Site.Biochemistry · 2023Article
- 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
- Linear Free Energy Relationships for Enzymatic Reactions: Fresh Insight from a Venerable Probe.Accounts of chemical research · 2021Review
- Gene Cloning, Recombinant Expression, Characterization, and Molecular Modeling of the Glycolytic Enzyme Triosephosphate Isomerase fromMicroorganisms · 2019Article
- The role of ligand-gated conformational changes in enzyme catalysis.Biochemical Society transactions · 2019Review
- Uncovering the Role of Key Active-Site Side Chains in Catalysis: An Extended Brønsted Relationship for Substrate Deprotonation Catalyzed by Wild-Type and Variants of Triosephosphate Isomerase.Journal of the American Chemical Society · 2019Article
- Phosphoglycolate has profound metabolic effects but most likely no role in a metabolic DNA response in cancer cell lines.The Biochemical journal · 2019Article
- 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
- First characterization of a microsporidial triosephosphate isomerase and the biochemical mechanisms of its inactivation to propose a new druggable target.Scientific reports · 2018Article
- A reevaluation of the origin of the rate acceleration for enzyme-catalyzed hydride transfer.Organic & biomolecular chemistry · 2017Review
- Enzyme activation through the utilization of intrinsic dianion binding energy.Protein engineering, design & selection : PEDS · 2017Review
- Article
- Enzyme Architecture: A Startling Role for Asn270 in Glycerol 3-Phosphate Dehydrogenase-Catalyzed Hydride Transfer.Biochemistry · 2016Article
- Linking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA).Chemical science · 2016Article
- Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Journal of the American Chemical Society · 2015Article
- The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture.Journal of the American Chemical Society · 2015Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Triosephosphate isomerase (TIM) catalyzes the isomerization of dihydroxyacetone phosphate to form d-glyceraldehyde 3-phosphate. The effects of two structural mutations in TIM on the kinetic parameters for catalysis of the reaction of the truncated substrate glycolaldehyde (GA) and the activation of this reaction by phosphite dianion are reported. The P168A mutation results in similar 50- and 80-fold decreases in (kcat/Km)E and (kcat/Km)E·HPi, respectively, for deprotonation of GA catalyzed by free TIM and by the TIM·HPO(3)(2-) complex. The mutation has little effect on the observed and intrinsic phosphite dianion binding energy or the magnitude of phosphite dianion activation of TIM for catalysis of deprotonation of GA. A loop 7 replacement mutant (L7RM) of TIM from chicken muscle was prepared by substitution of the archaeal sequence 208-TGAG with 208-YGGS. L7RM exhibits a 25-fold decrease in (kcat/Km)E and a larger 170-fold decrease in (kcat/Km)E·HPi for reactions of GA. The mutation has little effect on the observed and intrinsic phosphodianion binding energy and only a modest effect on phosphite dianion activation of TIM. The observation that both the P168A and loop 7 replacement mutations affect mainly the kinetic parameters for TIM-catalyzed deprotonation but result in much smaller changes in the parameters for enzyme activation by phosphite dianion provides support for the conclusion that catalysis of proton transfer and dianion activation of TIM take place at separate, weakly interacting, sites in the protein catalyst.
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