Enzyme kinetics

Enzyme kinetics is a field of chemistry. It describes how fast reactions happen, that involve enzymes. Enzyme kinetics is widely used in biology and chemistry. In enzyme kinetics, the reaction rate is measured, and the effects of different other factors of the environment are taken into account. Studying an enzyme this way can help people explain its role in the metabolism of animals and humans. It can also show how a certain substance or drug can affect this rate.

Enzyme Kinetics Media

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  Dihydrofolate reductase from E. coli with its two substrates dihydrofolate (right) and NADPH (left), bound in the active site. The protein is shown as a ribbon diagram, with alpha helices in red, beta sheathes in yellow and loops in blue. (Template:Pdb)

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  As larger amounts of substrate are added to a reaction, the available enzyme binding sites become filled to the limit of V_\max. Beyond this limit the enzyme is saturated with substrate and the reaction rate ceases to increase.

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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.

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  Lineweaver–Burk or double-reciprocal plot of kinetic data, showing the significance of the axis intercepts and gradient.

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  Random-order ternary-complex mechanism for an enzyme reaction. The reaction path is shown as a line and enzyme intermediates containing substrates A and B or products P and Q are written below the line.

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  Saturation curve for an enzyme reaction showing sigmoid kinetics.

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  Pre-steady state progress curve, showing the burst phase of an enzyme reaction.

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  Kinetic scheme for reversible enzyme inhibitors.

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  The energy variation as a function of reaction coordinate shows the stabilisation of the transition state by an enzyme.