Question

CI OD 17) Human alcohol dehydrogenase is capable of oxidizing several substrates besides ethanol. The kinetic parameters for these other substrates are given in the table below. Assume a constant enzyme amount of 1 mmol when these experimental values were obtained Use this table to answer questions 17a and 17b. note:UM = micromolar Substrate Km (UM) Vmax (mmol/min) Hexanol Butanol Ethylene Glycol Methanol Propanol

Answer 1

17a). Most preferred substarte is methanol.. Because

Km is the Michaelis-Menten constant which shows the concentration of the substrate when the reaction velocity is equal to one half of the maximal velocity for the reaction. It can also be thought of as a measure of how well a substrate complexes with a given enzyme, otherwise known as its binding affinity. An equation with a low Km value indicates a large binding affinity, as the reaction will approach Vmax more rapidly. An equation with a high Km indicates that the enzyme does not bind as efficiently with the substrate, and Vmax will only be reached if the substrate concentration is high enough to saturate the enzyme.

17b). Speficity constant is given by Kcat/Km is a measure of how efficiently an enzyme converts substrates into products.....