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Concept
Michaelis–Menten kinetics
Summary
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 an equation describing the rate reaction rate (rate of formation of product P, with concentration ) to , the concentration of the substrate A (using the symbols recommended by the IUBMB). Its formula is given by the Michaelis–Menten equation:
which is often written as , represents the limiting rate approached by the system at saturating substrate concentration for a given enzyme concentration. When the value of the Michaelis constant is numerically equal to the substrate concentration, the reaction rate is half of . Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions. Only a small proportion of enzyme-catalysed reactions have just one substrate, but the equation still often applies if only one substrate concentration is varied.
The plot of against has often been called a “Michaelis–Menten plot”, even recently, but this is misleading, because Michaelis and Menten did not use such a plot. Instead, they plotted against , which has some advantages over the usual ways of plotting Michaelis–Menten data. It has as dependent variable, and thus does not distort the experimental errors in . Michaelis and Menten did not attempt to estimate directly from the limit approached at high , something difficult to do accurately with data obtained with modern techniques, and almost impossible with their data. Instead they took advantage of the fact that the curve is almost straight in the middle range and has a maximum slope of i.e. . With an accurate value of it was easy to determine from the point on the curve corresponding to .
This plot is virtually never used today for estimating and , but it remains of major interest because it has another valuable property: it allows the properties of isoenzymes catalysing the same reaction, but active in very different ranges of substrate concentration, to be compared on a single plot.
Official source
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