The Catalytic Péclet Number: Michaelis-Menten Kinetics as Drift-Diffusion and the Thermodynamic Foundations of Enzyme Specificity
Abstract
Formally establishes that Michaelis-Menten enzyme kinetics has drift-diffusion structure: V_max is directed catalytic drift, K_m is substrate dissociation diffusion, and the catalytic efficiency k_cat/K_m is a Péclet number. Derives the channel conversion efficiency η_conv 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.
Fields of Study & Subjects
thermodynamics and calorimetric analyses
Diffusion and Search Dynamics
Protein Structure and Dynamics
Publication details
- Journal / source
- Zenodo (CERN European Organization for Nuclear Research)
- Publication date
- 26 February 2026
- Language
- EN
- Document type
- Preprint