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Progress curve for an enzyme reaction. The slope in the initial rate period is the initial rate of reaction v. The Michaelis–Menten equation describes how this slope varies with the concentration of substrate. Enzyme assays are laboratory procedures that measure the rate of enzyme reactions. Since enzymes are not consumed by the reactions ...
Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. 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.
File:Michaelis-Menten saturation curve of an enzyme reaction-ru.svg Derivative works of this file: Michaelis-Menten Sättigungskurve einer Enzymreaktion.svg Deutsch: file:Michaelis-Menten plot.svg
Enzymes however display a saturation effect where,, as the substrate concentration is increased the reaction rate reaches a maximum value. Standard approaches to describing this behavior are based on models developed by Michaelis and Menten as well and Briggs and Haldane .
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Plot of the % saturation of oxygen binding to haemoglobin, as a function of the amount of oxygen present (expressed as an oxygen pressure). Data (red circles) and Hill equation fit (black curve) from original 1910 paper of Hill. [6] The Hill equation is commonly expressed in the following ways: [2] [7] [8]
The Lineweaver–Burk plot derives from a transformation of the Michaelis–Menten equation, = + in which the rate is a function of the substrate concentration and two parameters , the limiting rate, and , the Michaelis constant.