Enzyme Kinetics Please explain reasoning for answers.
How does the [S] affect the rate of an enzymatic reaction? Why don’t enzyme catalyzed rates increase linearly with [S]?
How will Km (Michaelis Constant) it affect the rate of an enzymatic reaction? What will it change on the hyperbolic curve? Why is the kcat/Km ratio a superior way to compare one enzyme to another as compared to either of the two constants alone?
What happens to the Michaelis-Menten equation when [S] << Km? When [S] >> Km and when [S] = Km?
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