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Question

The half-maximal velocity of an enzyme catalyzed reaction was found at a substrate concentration of 0.5 × 10 ⁻⁶ M. This enzyme follows Michaelis-Menten kinetics. In the presence of a competitive inhibitor, the half-maximal velocity was found at a substrate concentration of 1.5 × 10 ⁻⁶ M. Given that the enzymeinhibitor pair has a dissociation constant of 2 × 10 ⁻⁶ M the concentration of the competitive inhibitor in μ𝑀, rounded off to one place of decimal, was_____. (NAT)

Explanation

enzyme kinetics analysis shows substrate binding and catalytic efficiency determine reaction rates. Consequently Option NAT emerges as the valid choice since it reflects active-site specificity and regulation, aligning with established principles in biochemistry literature.

Discussion

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