BioChemistry > Lab Report > Arizona State University - BCH 367enzyme kinetics lab CH (All)
Enzyme Kinetics Lab BCH 367 Introduction The purpose of this experiment is to use Michaelis Menten kinetics calculations as well as graphs obtained using the calculations to determine Vmax, the ma... ximum rate of reaction and Km, which describes how well the substrate binds to the enzyme. In the enzyme kinetics experiment, Michaelis Menten kinetics is used to derive an understanding of how enzymes work as catalysts in biochemical reactions. All reactions have a rate and this rate is dependent on several factors. Understanding the kinetics of the reaction can serve as the foundation to comprehending the catalytic nature of enzymes. The Michaelis Menten equation is v=Vmax[S]/Km+[S] where v is the reaction rate, Vmax the maximum rate of reaction where the enzyme is saturated with substrate, Km, Michaelis constant, is the substrate concentration where the reaction velocity (v) is ½ Vmax. [S] is the substrate concentration. This model relates reaction velocity to substrate concentration. When a substrate (S) binds to an enzyme (E) it forms an enzyme-substrate complex ES which is reversible. However, once it reacts irreversibly it will generate a product (P) and [Show More]
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