ArticleACS catalysis2017
Shuffling Active Site Substate Populations Affects Catalytic Activity: The Case of Glucose Oxidase.
Article in ACS catalysis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 71 citations in OpenAlex.
- Substrate-Specific Differences in Catalytic Strategy and Activity across Ketol-Acid Reductoisomerase Variants.The journal of physical chemistry. B · 2026Article
- Why Do PETases Struggle with Crystalline PET? Catalytic Ensemble Sampling Reveals Molecular Bottlenecks.The journal of physical chemistry letters · 2026Article
- Revealing the intricate mechanism governing the pH-dependent activity of a quintessential representative of flavoproteins, glucose oxidase.Fundamental research · 2026Article
- Glucose Oxidase Initiates Radical Polymerizations by Direct Electron Transfer to Monomers.Biomacromolecules · 2025Article
- Modification and applications of glucose oxidase: optimization strategies and high-throughput screening technologies.World journal of microbiology & biotechnology · 2025Review
- Substrate Turnover Dynamics Guide Ketol-Acid Reductoisomerase Redesign for Increased Specific Activity.ACS catalysis · 2024Article
- Kinetically restrained oxygen reduction to hydrogen peroxide with nearly 100% selectivity.Nature communications · 2022Article
- Glucose Oxidase, an Enzyme "Ferrari": Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications.Biomolecules · 2022Review
- Ultrafast photooxidation of protein-bound anionic flavin radicals.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Fuel-Driven and Enzyme-Regulated Redox-Responsive Supramolecular Hydrogels.Angewandte Chemie (International ed. in English) · 2021Article
- Two β-Lactamase Variants with Reduced Clavulanic Acid Inhibition Display Different Millisecond Dynamics.Antimicrobial agents and chemotherapy · 2021Article
- Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020Review
- Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulations.PLoS computational biology · 2019Article
- Enzymatic self-wiring in nanopores and its application in direct electron transfer biofuel cells.Nanoscale advances · 2019Article
- The evolution of multiple active site configurations in a designed enzyme.Nature communications · 2018Article
- Conformational dynamics and enzyme evolution.Journal of the Royal Society, Interface · 2018Review
- Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis.ACS catalysis · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Glucose oxidase has wide applications in the pharmaceutical, chemical, and food industries. Many recent studies have enhanced key properties of this enzyme using directed evolution, yet without being able to reveal why these mutations are actually beneficial. This work presents a synergistic combination of experimental and computational methods, indicating how mutations, even when distant from the active site, positively affect glucose oxidase catalysis. We have determined the crystal structures of glucose oxidase mutants containing molecular oxygen in the active site. The catalytically important His516 residue has been previously shown to be flexible in the wild-type enzyme. The molecular dynamics simulations performed in this work allow us to quantify this floppiness, revealing that His516 exists in two states: catalytic and noncatalytic. The relative populations of these two substates are almost identical in the wild-type enzyme, with His516 readily shuffling between them. In the glucose oxidase mutants, on the other hand, the mutations enrich the catalytic His516 conformation and reduce the flexibility of this residue, leading to an enhancement in their catalytic efficiency. This study stresses the benefit of active site preorganization with respect to enzyme conversion rates by reducing molecular reorientation needs. We further suggest that the computational approach based on Hamiltonian replica exchange molecular dynamics, used in this study, may be a general approach to screening in silico for improved enzyme variants involving flexible catalytic residues.
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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.