Enzyme Kinetics and Inhibitors

Enzymes Kinetics and Inhibitors Factors Affecting Enzymatic Reaction 

The factors that mainly influence any enzyme-catalysed reaction are  

Other factors such as state of enzyme (oxidation), time and activators also affect enzyme-catalysed reaction to certain extent. 

Keeping the factors such as pH, temperature and enzyme concentration at optimum levels, if the substrate concentration is increased, the velocity of the reaction recorded a rectangular hyperbola. At very low substrate concentration the initial reaction velocity (v) is nearly proportional to the substrate concentration (first order kinetics). However, if the substrate concentration is increased the rate of increase slows down (mixed order kinetics). With a further increase in the subshate concentration the reaction rate approaches a constant (zero order-reaction where velocity is independent of substrate concentration). 

At initial point, eventhough the substrate molecules are present in excess than enzyme on molar basis, not all the enzyme molecules present combine with the 

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Abstract Neuroscientists may wish to quantify an enzyme activity for one of many reasons. In order to do so, the researcher must be able to set up an assay appropriately, and this requires some understanding of the kinetic behavior of the enzyme toward the substrate used. Furthermore, such an understanding is vital if the inhibitory effects of a drug are to be assessed appropriately. This chapter outlines key principles that must be adhered to, and describes basic approaches by which rather complex kinetic data might be obtained, in order that enzyme kinetics and inhibitor kinetics might be studied successfully by the nonexpert. 

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