ArticleThe Journal of chemical physics2011
Michaelis-Menten relations for complex enzymatic networks.
Article in The Journal of chemical physics, 2011. 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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Who cites it
7 citing papers in PubMed.
- High-order Michaelis-Menten equations allow inference of hidden kinetic parameters in enzyme catalysis.Nature communications · 2025Article
- Feasibility of a Novel Mobile C-Reactive Protein-Testing Device Using Gold-Linked Electrochemical Immunoassay: Clinical Performance Study.JMIR mHealth and uHealth · 2020Article
- Structural conditions on complex networks for the Michaelis-Menten input-output response.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Dependence of the Enzymatic Velocity on the Substrate Dissociation Rate.The journal of physical chemistry. B · 2017Article
- Enzymatic turnover of macromolecules generates long-lasting protein-water-coupled motions beyond reaction steady state.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Motor proteins and molecular motors: how to operate machines at the nanoscale.Journal of physics. Condensed matter : an Institute of Physics journal · 2013Review
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Abstract
Most biological processes are controlled by complex systems of enzymatic chemical reactions. Although the majority of enzymatic networks have very elaborate structures, there are many experimental observations indicating that some turnover rates still follow a simple Michaelis-Menten relation with a hyperbolic dependence on a substrate concentration. The original Michaelis-Menten mechanism has been derived as a steady-state approximation for a single-pathway enzymatic chain. The validity of this mechanism for many complex enzymatic systems is surprising. To determine general conditions when this relation might be observed in experiments, enzymatic networks consisting of coupled parallel pathways are investigated theoretically. It is found that the Michaelis-Menten equation is satisfied for specific relations between chemical rates, and it also corresponds to a situation with no fluxes between parallel pathways. Our results are illustrated for a simple model. The importance of the Michaelis-Menten relationship and derived criteria for single-molecule experimental studies of enzymatic processes are discussed.
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