# Enzyme kinetics at the molecular level

Source: [Enzyme kinetics at the molecular level](<https://www.sota2.com/research/paper/68fa39ae1e209131ce8c4a71>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-24T23:38:19.229Z

Authors: Arti Dua

Published: 2019-05-08T11:01:25.000Z

## 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 mini-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 unobservably short in the classical limit.

## Recorded benchmark results

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/1905.03005>)

[PDF](<https://arxiv.org/pdf/1905.03005.pdf>)