Question:
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\(^{-1}\) dm\(^{3}\) s and a slope of 2.10 s. The correct Michaelis constant for the reaction is ______ (rounded off to 2 decimal places).
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\(^{-1}\) dm\(^{3}\) s and a slope of 2.10 s. The correct Michaelis constant for the reaction is ______ (rounded off to 2 decimal places).
Updated On: Jul 20, 2024
- 5.88 mmol dm\(^{-3}\)
- 5.88 mmol dm\(^{-3}\) s\(^{-1}\)
- 2.80 mmol dm\(^{-3}\)
- 2.80 mmol dm\(^{-3}\) s\(^{-1}\)
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The Correct Option is A
Solution and Explanation
The correct option is (A) :5.88 mmol dm\(^{-3}\).
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