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Biochemistry Question on Enzyme kinetics

An enzyme-catalyzed conversion of a substrate at 298 K proceeds by a Michaelis-Menten mechanism. The Lineweaver-Burk plot for the analysis of the experimental data has an intercept along the y-axis of 0.357 mmol−1^{-1} dm3^{3} s and a slope of 2.10 s. The correct Michaelis constant for the reaction is ______ (rounded off to 2 decimal places).

A

5.88 mmol dm−3^{-3}

B

5.88 mmol dm−3^{-3} s−1^{-1}

C

2.80 mmol dm−3^{-3}

D

2.80 mmol dm−3^{-3} s−1^{-1}

Answer

5.88 mmol dm−3^{-3}

Explanation

Solution

The correct option is (A) :5.88 mmol dm−3^{-3}.