ArticleThe Journal of biological chemistry2008
Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- AFM for Studying the Functional Activity of Enzymes.Biomolecules · 2025Review
- Development of Single Molecule Techniques for Sensing and Manipulation of CRISPR and Polymerase Enzymes.Small (Weinheim an der Bergstrasse, Germany) · 2023Review
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Computational enzyme design approaches with significant biological outcomes: progress and challenges.Computational and structural biotechnology journal · 2012Review
- Probing the mutational interplay between primary and promiscuous protein functions: a computational-experimental approach.PLoS computational biology · 2012Article
- Single-molecule paleoenzymology probes the chemistry of resurrected enzymes.Nature structural & molecular biology · 2011Article
- Single-molecule force spectroscopy approach to enzyme catalysis.The Journal of biological chemistry · 2010Review
- Exploring the contribution of collective motions to the dynamics of forced-unfolding in tubulin.Biophysical journal · 2010Article
- Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy.Nature structural & molecular biology · 2009Article
- Mechanochemistry: one bond at a time.ACS nano · 2009Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Understanding how the catalytic mechanisms of enzymes are optimized through evolution remains a major challenge in molecular biology. The concept of co-evolution implicates that compensatory mutations occur to preserve the structure and function of proteins. We have combined statistical analysis of protein sequences with the sensitivity of single molecule force-clamp spectroscopy to probe how catalysis is affected by structurally distant correlated mutations in Escherichia coli thioredoxin. Our findings show that evolutionary anti-correlated mutations have an inhibitory effect on enzyme catalysis, whereas positively correlated mutations rescue the catalytic activity. We interpret these results in terms of an evolutionary tuning of both the enzyme-substrate binding process and the chemistry of the active site. Our results constitute a direct observation of distant residue co-evolution in enzyme catalysis.
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Registered trials
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