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.. The more scientists understand the workings of enzymes, the better they understand the complex array of reactions that make up the web of life, in healthy and in diseased states. Seminal work published in 1912 by Leonor Michaelis (1875-1949) and Maud Leonora Menten (1879-1960), a German man and a Canadian woman, cast light on the reasons.

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Significance of k m in Michaelis Menten equation. The K m is Michaelis constant and it can be defined as the substrate concentration at which the rate of reaction is half of the maximum velocity(V max).K m represents the affinity of an enzyme for a particular substrate. It means the lower the value of K m, the greater the enzyme's affinity for the substrate.. The Michaelis-Menten Equation describes the relationship between the rate of an enzyme-catalyzed reaction and the concentration of the substrate. It was named after the scientists Leonor Michaelis and Maud Menten, who developed it in 1913. If you've read about kinetics, these words may sound familiar. That's because enzyme-substrate.