BIOCHEMISTRY
ENZYMES AND METABOLISM
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Question
[CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
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At zero concentration of substrate, meaning [S]=0, the velocity is zero
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As the concentration of the substrate increases, the formation of product also increases
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The plot is generated using different concentration of substrate
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The plot is generated using different concentration of enzyme
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Detailed explanation-1: -1. Which of the following is true about Michaelis-Menten kinetics? Explanation: Km is defined as the concentration of substrate at which enzyme is working at half of maximum velocity. It is also a measure of the affinity that the enzyme has for its substrate.
Detailed explanation-2: -In a Michaelis-Menten plot of enzyme kinetics, the reaction rate is plotted as a function of substrate concentration. Why is it that as substrate concentration increases, the curve of the graph levels off and reaches a plateau?
Detailed explanation-3: -Three assumptions are implicit in Michaelis-Menten kinetics: the steady-state approximation, the free ligand approximation and the rapid equilibrium approximation.
Detailed explanation-4: -1 Answer. For explanation I would say: The breakdown of ES complex is the rate determining step of Michaelis Menten kinetics.