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

The classical Michaelis-Menten equation assumes that the Michaelis constant (Km) is independent of enzyme concentration. However, this study presents a novel theoretical framework suggesting that Km increases with enzyme concentration due to electrostatic and steric effects influencing substrate binding. By analyzing kinetic data and mathematical modeling, we demonstrate that traditional approximations such as the quasi-steady-state assumption (QSSA) and reactant stationary approximation (RSA) may not fully describe enzymatic behavior under varying enzyme concentrations. Our findings suggest a fundamental revision in enzyme kinetics, with potential applications in metabolic regulation and drug development. The implications extend to the design of enzyme inhibitors, particularly in therapeutic strategies targeting metabolic pathways in diseases such as cancer and autoimmune disorders. This paradigm shift challenges conventional enzymology and provides new perspectives on enzyme-substrate interactions.