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In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1] For enzymes with a single active site, k cat is referred to as the catalytic constant. [2]
Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1.The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule.
The apparent unimolecular rate constant k cat is also called turnover number, and denotes the maximum number of enzymatic reactions catalysed per second. The Michaelis–Menten equation [10] describes how the (initial) reaction rate v 0 depends on the position of the substrate-binding equilibrium and the rate constant k 2.
The Michaelis-Menten constant is denoted by K m and is represented by the equation K m = (K off + K cat)/ K on [definition needed]. The rates that the enzyme binds and dissociates from the substrate are represented by K on and K off respectively. K m is also defined as the substrate concentration at which enzymatic velocity reaches half of its ...
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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.
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