The rate limiting step in the enzyme catalyzed
transformation of substrate S into product P is the breakdown of the ES
complex:
Since the ES concentration is
not easily measured experimentally, Leonor Michaelis and Maud Menten
have given an alternative expression for the determination of the rate
of such enzymatic reactions:
where KM,
the Michaelis constant is defined as: 
Several algebraic transformations to a linear form have been proposed for this equation which are more useful in the analysis of the experimental data: Lineweaver-Burk, Eadie and Dixon.
Given the following data for the hydrolysis of sucrose by the enzyme invertase, find which equation has the best correlation coefficient, determine the Michaelis constant and kb - the maximum turnover number:
| [S] | 0.0292 | 0.0584 | 0.0876 | 0.117 | 0.146 | 0.146 | 0.175 | 0.234 |
| k | 0.182 | 0.265 | 0.311 | 0.330 | 0.349 | 0.349 | 0.372 | 0.371 |
In the Dixon expression, which has the best correlation, the substrate concentration [S] is correlated to the ratio of the substrate concentration [S] to the rate k. The maximum turnover number is the reciprocal of the slope, and the Michaelis constant is the product of the intercept with the maximum turnover number.
Question:
