Enzyme kinetics and the maximum entropy production principle

A general proof is derived that entropy production can be maximized with respect to rate constants in any enzymatic transition. This result is used to test the assumption that biological evolution of enzyme is accompanied with an increase of entropy production in its internal transitions and that such increase can serve to quantify the progress of enzyme evolution. The state of maximum entropy production would correspond to fully evolved enzyme. As an example the internal transition ES ↔ EP in a generalized reversible Michaelis–Menten three state scheme is analyzed. A good agreement is found among experimentally determined values of the forward rate constant in internal transitions ES → EP for three types of β-Lactamase enzymes and their optimal values predicted by the maximum entropy production principle, which agrees with earlier observations that β-Lactamase enzymes are nearly fully evolved. The optimization of rate constants as the consequence of basic physical principle, which is the subject of this paper, is a completely different concept from a) net metabolic flux maximization or b) entropy production minimization (in the static head state), both also proposed to be tightly connected to biological evolution. [Display omitted] ► Optimization of a single transition rate constant using the MEP principle. ► Application to the intraenzymatic transition of a three state enzyme reaction. ► Comparison with measured rate constants for β-Lactamases.