Enzyme kinetics is the study of the chemical reactions that are catalyzed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or an agonist might inhibit the enzyme. Creative Enzymes is a renowned service provider, supporting many industrial and academic researchers for kinetic studies. This service helps to determine virtually all kinetic parameters such as V_max, K_d, K_M, k_cat, k_a, and k_b.

In an enzymatic reaction, the substrate molecules bind to an enzyme's active site and are transformed into products through a series of steps described in the enzymatic mechanism.

E + S ↔ ES ↔ ES* ↔ EP ↔ E + P

These mechanisms can be divided into single-substrate and multiple-substrate mechanisms. Enzyme kinetic studies on enzymes that only bind one substrate, such as triosephosphate isomerase, aim to measure the affinity with which the enzyme binds this substrate and the turnover rate. When enzymes bind multiple substrates, such as dihydrofolate reductase, enzyme kinetics can also show the sequence in which these substrates bind and the sequence in which products are released.

The workflow of enzyme kinetic studies

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