K Cat Formula

Studying an enzyme s kinetics in this way 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.

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. K cat k d and k m k cat k d and k m are terms helpful in the description of an enzyme that follows the michaelis menten kinetics. 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.

Robert roskoski in xpharm. The turnover number of an enzyme or the k cat is the maximal number of molecules of substrate converted to product per active site per unit time when the enzyme is saturated with substrate garrett and grisham 1999 this value is calculated from the maximal velocity. The comprehensive pharmacology reference 2007. Computing kcat by hand.

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. 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. 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. K d is dissociation constant.

It is expressed in the same units you used to enter your y values enzyme activity. 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.