On the Velocity of Enzymatic Reactions in Michaelis–Menten-Like Schemes (Ensemble and Single-Molecule Versions)

Abstract

In searching non-standard ways of conformational regulation, various Michaelis–Menten-like schemes attract relentless attention, resulting in sometimes too sophisticated considerations. With the example of monomeric enzymes possessing an only binding site, we define the minimal schemes capable of bearing peculiar regulatory properties like “cooperativity” or substrate inhibition. The simplest ways of calculating the enzymatic reaction velocity are exemplified, either in the ensemble or single-molecule case.