ArticleScientific reports2015
Variance-corrected Michaelis-Menten equation predicts transient rates of single-enzyme reactions and response times in bacterial gene-regulation.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 27 citations in OpenAlex.
- Putting theory to the test: An integrated computational/experimental chemostat model of the tragedy of the commons.PloS one · 2024Article
- Substantial gradient mitigation in simulated large-scale bioreactors by optimally placed multiple feed points.Biotechnology and bioengineering · 2022Article
- Extensions to Michaelis-Menten Kinetics for Single Parameters.Scientific reports · 2018Article
- One-Dimensional Search Dynamics of Tumor Suppressor p53 Regulated by a Disordered C-Terminal Domain.Biophysical journal · 2017Article
- Article
- Regiospecific synthesis of prenylated flavonoids by a prenyltransferase cloned from Fusarium oxysporum.Scientific reports · 2016Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many chemical reactions in biological cells occur at very low concentrations of constituent molecules. Thus, transcriptional gene-regulation is often controlled by poorly expressed transcription-factors, such as E.coli lac repressor with few tens of copies. Here we study the effects of inherent concentration fluctuations of substrate-molecules on the seminal Michaelis-Menten scheme of biochemical reactions. We present a universal correction to the Michaelis-Menten equation for the reaction-rates. The relevance and validity of this correction for enzymatic reactions and intracellular gene-regulation is demonstrated. Our analytical theory and simulation results confirm that the proposed variance-corrected Michaelis-Menten equation predicts the rate of reactions with remarkable accuracy even in the presence of large non-equilibrium concentration fluctuations. The major advantage of our approach is that it involves only the mean and variance of the substrate-molecule concentration. Our theory is therefore accessible to experiments and not specific to the exact source of the concentration fluctuations.
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