ArticlePloS one2014
Asymmetric effect of mechanical stress on the forward and reverse reaction catalyzed by an enzyme.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 17 citations in OpenAlex.
- Article
- The enzyme activity of mitochondrial trifunctional protein is not altered by lysine acetylation or lysine succinylation.PloS one · 2021Article
- Determinants of cyclization-decyclization kinetics of short DNA with sticky ends.Nucleic acids research · 2020Article
- A force sensor that converts fluorescence signal into force measurement utilizing short looped DNA.Biosensors & bioelectronics · 2018Article
- Green function of correlated genes in a minimal mechanical model of protein evolution.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Modulation of DNA loop lifetimes by the free energy of loop formation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- On the Origin of Hemoglobin Cooperativity under Non-equilibrium Conditions.Discoveries (Craiova, Romania)Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The concept of modulating enzymatic activity by exerting a mechanical stress on the enzyme has been established in previous work. Mechanical perturbation is also a tool for probing conformational motion accompanying the enzymatic cycle. Here we report measurements of the forward and reverse kinetics of the enzyme Guanylate Kinase from yeast (Saccharomyces cerevisiae). The enzyme is held in a state of stress using the DNA spring method. The observation that mechanical stress has different effects on the forward and reverse reaction kinetics suggests that forward and reverse reactions follow different paths, on average, in the enzyme's conformational space. Comparing the kinetics of the stressed and unstressed enzyme we also show that the maximum speed of the enzyme is comparable to the predictions of the relaxation model of enzyme action, where we use the independently determined dissipation coefficient [Formula: see text] for the enzyme's conformational motion. The present experiments provide a mean to explore enzyme kinetics beyond the static energy landscape picture of transition state theory.
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