Characterize Enzyme Kinetics

Enzymes are proteins that operate as biological catalysts, which have an important role in the biochemical activities that occur in living organisms. For biochemists, a primary focus of research is understanding the function of enzymes, and how to inhibit or activate their activity.

As a number of drug targets are enzymes, the production of novel therapies requires knowledge of how the target enzyme catalyzes and binds its natural substrate.

Multiple drugs are therapeutic enzymes, which are injected into the patient to remedy genetic disorders caused by defective or missing enzymes. Enzymes are also crucial in additional industries such as detergents, biofuels, and food science.

While enzymes were found in the mid-1800s, purified and isolated since the early 20th century, and expressed and cloned in recombinant systems since the 1970s, there is a constant demand for complex and efficient enzyme research to utilize the potential of enzyme-driven catalytic reactions.

Novel enzymes are also being identified. Dependable enzyme kinetics data are critical to control and understand the effectiveness of enzymes and to produce pioneering drugs.

Isothermal titration calorimetry (ITC) methods have been effectively utilized in the study of enzyme inhibition and kinetics. ITC is a versatile, well-established technique that is predominantly used for the measurement of reaction thermodynamics.

This article outlines how ITC provides real-time, enzyme kinetics data, in comparison to alternative enzyme assays. In part 2, how to perform enzyme kinetics investigations with a MicroCal ITC system is outlined.

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This information has been sourced, reviewed and adapted from materials provided by Malvern Panalytical.

For more information on this source, please visit Malvern Panalytical.

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