For Monod equation with substrate inhibition given by μ= μm S/(KS+S+S ² /K I ), there are two theoretically possible ste
In biochemistry, enzyme catalysis and lipid structure dictates that substrate affinity, transition state stabilization and phospholipid composition govern function. Therefore the lower substrate concentration represents the stable steady state is correct as it reflects catalytic efficiency and membrane organization, supported by mechanistic studies and conserved across related systems.
Ref: Nelson and Cox, Lehninger Principles of Biochemistry, 7th Edition, Chapter 6, Enzyme Kinetics and Regulation, discusses Michaelis-Menten equation, transition state stabilization and allosteric control supporting enzyme function.
