# Asymmetric enzyme kinetics of F1-ATPase induced by rotation-assisted substrate binding

Source: [Asymmetric enzyme kinetics of F1-ATPase induced by rotation-assisted substrate binding](<https://www.sota2.com/research/paper/68fa4a6f1e209131ce93e690>)

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

Data updated: 2025-10-27T04:38:04.564Z

Authors: Yohei Nakayama, Shoichi Toyabe

Published: 2024-02-27T09:02:30.000Z

## Abstract

We demonstrate asymmetric enzyme kinetics of a biomolecular motor F1-ATPase between synthesis and hydrolysis of adenosine triphosphate (ATP). Our experiments show that ATP hydrolysis follows Michaelis-Menten kinetics, but ATP synthesis, which is an F1-ATPase's primary biological role, deviates from it. Specifically, the synthesis rate is sustained even at low substrate concentrations. Analysis of a theoretical model consistent with the experimental results reveals that ATP synthesis implements a rotation-assisted mechanism, in which a limited binding rate at low substrate concentration is partially compensated for by rotation to an angle where the binding rate is high. The results may imply that F1-ATPase implements a regulatory mechanism of enhancing substrate binding for ATP synthesis.

## Recorded benchmark results

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/2402.17326>)

[PDF](<https://arxiv.org/pdf/2402.17326.pdf>)