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Enzyme Kinetics at the Molecular Level

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Abstract

The celebrated Michaelis-Menten (MM) expression provides a fundamental relation between the rate of enzyme catalysis and substrate concentration. The validity of this classical expression is, however, restricted to macroscopic amounts of enzymes and substrates and, thus, to processes with negligible fluctuations. Recent experiments have measured fluctuations in the catalytic rate to reveal that the MM equation, though valid for bulk amounts, is not obeyed at the molecular level. In this review, we show how new statistical measures of fluctuations in the catalytic rate identify a regime in which the MM equation is always violated. This regime, characterized by temporal correlations between enzymatic turnovers, is absent for a single enzyme and is unobservably short in the classical limit.

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Correspondence to Arti Dua.

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Arti Dua is an Associate Professor in the Indian Institute of Technology Madras. She is a theoretical chemist, working in the area of stochastic reaction dynamics and statistical mechanics of complex fluids.

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Dua, A. Enzyme Kinetics at the Molecular Level. Reson 24, 297–311 (2019). https://doi.org/10.1007/s12045-019-0781-9

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  • DOI: https://doi.org/10.1007/s12045-019-0781-9

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