Using this assumption, one can derive the Michaelis-Menten equation . The Michaelis-Menten equation describes a rectangular hyperbola. The turnover number of an enzyme, k cat , is the maximal velocity per enzyme molecule per unit of time. M is also the best way to determine the specificity of an enzyme. For hydrolysis of a peptide bond by the proteolytic enzyme chymotrypsin, the nature of the R 1 sidechain is critical .
Many enzymatic reactions involve more than one substrate.
Although the kinetics are complex, they can be very informative about the mechanism. A brief overview is give here . Amount of substrate. Control of activity. Multisubunit enzymes Homoallostery - cooperative substrate binding and activation.