ArticleScience (New York, N.Y.)2011
A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis.
Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 234 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
234 citing papers in PubMed, 461 citations in OpenAlex.
- Detecting Vibrational Energy Transfer into an Enzyme Active Site via a Transition State Analog.The journal of physical chemistry letters · 2026Article
- Fast Motions in 5 Alpha Reductase and Its Impact on Enzyme Kinetics.ACS catalysis · 2026Article
- Tryptophanase Mining and Characterization toward the Biological Production of Indole Derivatives.ACS omega · 2026Article
- Site-resolved energetic information from HX-MS experiments.Nature chemical biology · 2026Article
- Mapping functional dynamics hotspots for protein engineering with NMR peak intensity analysis.Protein engineering, design & selection : PEDS · 2026Article
- Fast product release requires active-site water dynamics in carbonic anhydrase.Nature communications · 2025Article
- A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025Review
- Conformational flexibility associated with remote residues regulates the kinetic properties of glutamate dehydrogenase.Protein science : a publication of the Protein Society · 2025Article
- Dynamic energy conversion in protein catalysis: From brownian motion to enzymatic function.Computational and structural biotechnology journal · 2025Review
- Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase.The journal of physical chemistry. B · 2024Article
- Electrostatic Preorganization in Three Distinct Heterogeneous Proteasome β-Subunits.ACS catalysis · 2024Article
- Article
- In Silico Drug Repurposing Endorse Amprenavir, Darunavir and Saquinavir to Target Enzymes of Multidrug Resistant UropathogenicIndian journal of microbiology · 2024Article
- Article
- Statistical Coupling Analysis Predicts Correlated Motions in Dihydrofolate Reductase.bioRxiv : the preprint server for biology · 2024Article
- Article
- Solution Ionic Strength Can Modulate Functional Loop Conformations inThe journal of physical chemistry. B · 2024Article
- Electrostatics as a Guiding Principle in Understanding and Designing Enzymes.Journal of chemical theory and computation · 2024Review
- A unified view on enzyme catalysis by cryo-EM study of a DNA topoisomerase.Communications chemistry · 2024Article
- Perturbative diffraction methods resolve a conformational switch that facilitates a two-step enzymatic mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
174 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Conformational dynamics play a key role in enzyme catalysis. Although protein motions have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme catalysis has not been clearly established. We generated a mutant of Escherichia coli dihydrofolate reductase that abrogates millisecond-time-scale fluctuations in the enzyme active site without perturbing its structural and electrostatic preorganization. This dynamic knockout severely impairs hydride transfer. Thus, we have found a link between conformational fluctuations on the millisecond time scale and the chemical step of an enzymatic reaction, with broad implications for our understanding of enzyme mechanisms and for design of novel protein catalysts.
Indexed as
Identifiers
What OpenQuestion holds
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.