QuestionSBA
QuestionChoice
In competitive inhibition, Vmax remains the same. Competitive inhibitors compete with the substrate for the active site of an enzyme but do not affect the maximum rate of the enzyme-catalysed reaction.
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b
Vmax is decreased
QuestionChoice
Vmax is unaffected because competitive inhibitors do not alter an enzyme's maximal catalytic capacity. Instead, they primarily affect the affinity of an enzyme for its substrate. This can easily be overcome by increasing the concentration of the substrate.
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a
Vmax is unaffected
QuestionChoice
Competitive inhibition does not lead to an increase in Vmax. It specifically affects the affinity of an enzyme for its substrate but not the maximum rate of the reaction.
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c
Vmax is increased
QuestionChoice
Competitive inhibition does not directly inhibit Vmax. Instead, it reduces the effectiveness of the enzyme-substrate interaction by competing with the substrate for the active site.
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d
Vmax is partially inhibited
QuestionChoice
This is a general statement that applies to Michaelis-Menten kinetics, but it is not specific to competitive inhibition. Competitive inhibition primarily affects the Km (Michaelis constant), which is a measure of the affinity of an enzyme for its substrate, and not the Vmax.
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e
Vmax is inversely proportional to substrate concentration
Concept
Chapter
2693
5712
Enzyme Kinetics
Topic
180
Biochemistry
17195
What is the effect of a competitive inhibitor on the Vmax of an enzyme?
a