K Cat Formula

In enzymology turnover number also termed k cat is defined as the maximum number of chemical conversions of substrate molecules per second that a single catalytic site will execute for a given enzyme concentration for enzymes with two or more active sites.

K cat formula.

The ratio k cat k m often referred to as the specificity constant is a useful index for comparing the relative rates of an enzyme acting on alternative competing substrates. Which describe how affinite two reactants are in a reaction. Turnover number has two different meanings. It is expressed in the same units you used to enter your y values enzyme activity.

For enzymes with a single active site k cat is referred to as the catalytic constant. The comprehensive pharmacology reference 2007. However an alternative description catalytic efficiency is frequently used and on occasions misused to compare the reactivity of two enzymes acting on the same substrate. K cat is a constant that describes the turnover rate of an enzyme substrate complex to product and enzyme it is also the rate of catalyst with a particular substrate.

If you plot enzyme velocity as a function of subtrate concentration you can fit the data to the michaelis menten equation to determine the k m and v max. Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes in enzyme kinetics the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Computing kcat by hand. K d is dissociation constant.

The v max is the maximum enzyme velocity extrapolated out to very high concentrations of substrate. Robert roskoski in xpharm.