Formally establishes that Michaelis-Menten enzyme kinetics has drift-diffusion structure: Vₘax is directed catalytic drift, Kₘ is substrate dissociation diffusion, and the catalytic efficiency kcat/Kₘ is a Péclet number. Derives the channel conversion efficiency ηconv for enzymes, shows the specificity-activity tradeoff is the Fantasia Bound in chemical space, and establishes that enzyme maintenance energy is the T3 constraint cost. Provides falsifiable predictions testable against BRENDA database enzyme kinetics.
Anthony W. Eckert (Thu,) studied this question.