The Michaelis-Menten Approach to Enzyme KineticsMATHEMATICAL The enzyme b-methylaspartase...

The Michaelis-Menten Approach to Enzyme Kinetics

MATHEMATICAL The enzyme b-methylaspartase catalyzes the deamination of b-methylaspartate

mesaconate absorbs at 240 nm

[V. Williams and J. Selbin,J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm (A240). From the data in the following table, determine Km for the reaction. How does the method of calculation differ from that in Questions 1 and Questions 2?

Questions 1

MATHEMATICAL Determine the values of Km and Vmax for the decarboxylation of a β-keto acid given the following data.

Questions 2

MATHEMATICAL The kinetic data in the following table were obtained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase:

CO2 + H2O → HCO3 + H +

[H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)]. From these data, determine Km and Vmax for the reaction.