ArticleBiochemistry2009
Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase.
Article in Biochemistry, 2009. 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, 51 citations in OpenAlex.
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- Ribosome External Electric Field Regulates Metabolic Enzyme Activity: The RAMBO Effect.The journal of physical chemistry. B · 2024Article
- Dynamozones are the most obvious sign of the evolution of conformational dynamics in HIV-1 protease.Scientific reports · 2023Article
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- Characterization of the ExoU activation mechanism using EPR and integrative modeling.Scientific reports · 2020Article
- Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR.Journal of biomolecular NMR · 2020Article
- A computational study of the molecular basis of antibiotic resistance in a DXR mutant.Journal of computer-aided molecular design · 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
- Species-Specific Inactivation of Triosephosphate Isomerase from Trypanosoma brucei: Kinetic and Molecular Dynamics Studies.Molecules (Basel, Switzerland) · 2017Article
- Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase.Journal of the American Chemical Society · 2015Article
- Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion.Journal of physical organic chemistry · 2014Article
- Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces.Journal of the American Chemical Society · 2014Article
- The critical role of the loops of triosephosphate isomerase for its oligomerization, dynamics, and functionality.Protein science : a publication of the Protein Society · 2014Article
- Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase.Biochemistry · 2013Article
- Gates of enzymes.Chemical reviews · 2013Review
- A distal mutation perturbs dynamic amino acid networks in dihydrofolate reductase.Biochemistry · 2013Article
- Article
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- Predicting flexible loop regions that interact with ligands: the challenge of accurate scoring.Proteins · 2012Article
- An introduction to NMR-based approaches for measuring protein dynamics.Biochimica et biophysica acta · 2011Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The enzyme triosephosphate isomerase (TIM) has been used as a model system for understanding the relationship between protein sequence, structure, and biological function. The sequence of the active site loop (loop 6) in TIM is directly correlated with a conserved motif in loop 7. Replacement of loop 7 of chicken TIM with the corresponding loop 7 sequence from an archaeal homologue caused a 10(2)-fold loss in enzymatic activity, a decrease in substrate binding affinity, and a decrease in thermal stability. Isotope exchange studies performed by one-dimensional (1)H NMR showed that the substrate-derived proton in the enzyme is more susceptible to solvent exchange for DHAP formation in the loop 7 mutant than for WT TIM. TROSY-Hahn Echo and TROSY-selected R(1rho) experiments indicate that upon mutation of loop 7, the chemical exchange rate for active site loop motion is nearly doubled and that the coordinated motion of loop 6 is reduced relative to that of the WT. Temperature dependent NMR experiments show differing activation energies for the N- and C-terminal hinges in this mutant enzyme. Together, these data suggest that interactions between loop 6 and loop 7 are necessary to provide the proper chemical context for the enzymatic reaction to occur and that the interactions play a significant role in modulating the chemical dynamics near the active site.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.