The Michaelis-Menten equation (see below) is commonly used to study the kinetics of reaction catalysis by enzymes as well as the kinetics of transport by transporters. Typically, the rate of reaction (or reaction velocity) is experimentally measured at several substrate concentration values. The range of substrate concentrations is chosen such that very low reaction rates as well as saturating.. K two times ET instead of times ES would be equal to Vmax instead of being equal to Vo like you see at the top. I'll make some room here and then sub in K two ES for Vo and K two E total for Vmax and then we finally get to our end equation which is called the Michaelis-Menten Equation and is super important when we talk about enzyme kinetics.

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The modern definition of enzymology is synonymous with the Michaelis-Menten equation instituted by Leonor Michaelis and Maud Menten. Most textbooks, or chapters within, discussing enzymology start with the derivation of the equation under the assumption of rapid equilibrium (as done by Michaelis-Menten) or steady state (as modified by Briggs and Haldane) conditions to highlight the importance.. Michaelis-Menten kinetics. In biochemistry, Michaelis-Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product. It takes the form of a differential equation describing the reaction rate (rate of formation of product P, with.