Influence of enzyme concentration on the Michaelis-Menten constant: A new theory

Corresponding Author:

Ishaan Mehta
Faculty of Chemistry, Alexandru Ioan Cuza University of Iași, Romania
E-mail: yassinfadel44@gmail.com

Received: 13-Sept-2024, Manuscript No. fmci-24-147893; Editor assigned: 15-Sept-2024, PreQC No. fmci-24-147893(PQ); Reviewed: 17-Sept-2024, QC No. fmci-24-147893(Q); Revised: 25-Sept-2024, Manuscript No. fmci-24-147893(R); Published: 27-Sept-2024

Abstract

This study proposes a novel theory that challenges the traditional view of the Michaelis-Menten constant (Km) as a fixed value for a given enzyme-substrate pair. We explore the possibility that Km can be modulated by enzyme concentration. By analyzing the relationship between initial reaction velocity and substrate concentration at different enzyme concentrations, we observed a change in the apparent affinity constant (designated as Km1 and Km2). This seemingly contradicts the established theory , and we have proposed a new theory to explain this variation.