ArticleProceedings of the National Academy of Sciences of the United States of America2015
Mediation of donor-acceptor distance in an enzymatic methyl transfer reaction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 83 citations in OpenAlex.
- MutexaGPT: An Intuition-to-Design Translator for Physics-based Enzyme Engineering.Research square · 2026Article
- Physics-based modeling in the new era of enzyme engineering.Nature computational science · 2025Review
- Methyl transfer in psilocybin biosynthesis.Nature communications · 2024Article
- Curcumin in Cancer Prevention: Insights from Clinical Trials and Strategies to Enhance Bioavailability.Current pharmaceutical design · 2024Review
- High-throughput computational investigation of protein electrostatics and cavity for SAM-dependent methyltransferases.Protein science : a publication of the Protein Society · 2023Article
- Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts.Current opinion in structural biology · 2022Review
- Factors That Determine the Variation of Equilibrium and Kinetic Properties of QM/MM Enzyme Simulations: QM Region, Conformation, and Boundary Condition.Journal of chemical theory and computation · 2022Article
- 2'-O methylation of RNA cap in SARS-CoV-2 captured by serial crystallography.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Transition-State Vibrational Analysis and Isotope Effects for COMT-Catalyzed Methyl Transfer.Journal of the American Chemical Society · 2020Article
- Hydrogen deuterium exchange defines catalytically linked regions of protein flexibility in the catecholProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Examining the Origin of Catalytic Power of Catechol O-Methyltransferase.ACS catalysis · 2019Article
- Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-ACS catalysis · 2019Article
- Revealing quantum mechanical effects in enzyme catalysis with large-scale electronic structure simulation.Reaction chemistry & engineering · 2019Article
- Crystallographic and Computational Characterization of Methyl Tetrel Bonding in S-Adenosylmethionine-Dependent Methyltransferases.Molecules (Basel, Switzerland) · 2018Article
- Large-scale QM/MM free energy simulations of enzyme catalysis reveal the influence of charge transfer.Physical chemistry chemical physics : PCCP · 2018Article
- Engineered control of enzyme structural dynamics and function.Protein science : a publication of the Protein Society · 2018Review
- Insights on the Origin of Catalysis on Glycine N-Methyltransferase from Computational Modeling.Journal of the American Chemical Society · 2018Article
- Origins of Enzyme Catalysis: Experimental Findings for C-H Activation, New Models, and Their Relevance to Prevailing Theoretical Constructs.Journal of the American Chemical Society · 2017Article
- Catechol-O-Methyltransferase and UDP-Glucuronosyltransferases in the Metabolism of Baicalein in Different Species.European journal of drug metabolism and pharmacokinetics · 2017Article
- Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Enzymatic methyl transfer, catalyzed by catechol-O-methyltransferase (COMT), is investigated using binding isotope effects (BIEs), time-resolved fluorescence lifetimes, Stokes shifts, and extended graphics processing unit (GPU)-based quantum mechanics/molecular mechanics (QM/MM) approaches. The WT enzyme is compared with mutants at Tyr68, a conserved residue that is located behind the reactive sulfur of cofactor. Small (>1) BIEs are observed for an S-adenosylmethionine (AdoMet)-binary and abortive ternary complex containing 8-hydroxyquinoline, and contrast with previously reported inverse (<1) kinetic isotope effects (KIEs). Extended GPU-based computational studies of a ternary complex containing catecholate show a clear trend in ground state structures, from noncanonical bond lengths for WT toward solution values with mutants. Structural and dynamical differences that are sensitive to Tyr68 have also been detected using time-resolved Stokes shift measurements and molecular dynamics. These experimental and computational results are discussed in the context of active site compaction that requires an ionization of substrate within the enzyme ternary complex.
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Registered trials
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.