An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min−110 µmol⋅min−1 when the substrate concentration is five times greater than the ?M.KM. What is the ?maxVmax of this enzyme?

The rate constants of an enzyme-catalyzed reaction, obeying the Michaelis-Menten kinetics, have been determined : E + S K₁ = 2 x 108 M-¹ S-¹ -1 -1 -1 K-₁= 1 x 10³ S K₂ = 5 x 10³ S-1 K₁ 1 K-1 ES K₂ E +P 1- Determine the Michaelis constant Km of the enzyme. 2- Determine the catalytic constant (kcat) of the enzyme. 3- Determine the catalytic efficiency of the enzyme.

The typical Michaelis-Menten equation mathematically describes the overall rate of the reaction as V (this is because biologists don't like math). What does V actually mean? (write the definition of V in differential equation form). V= d( )/dt Reaction rate Substrate concentration V max ·½V TURK

Which of the following statements are true about the relationships of [S], KM, and Vmax?  (Choose all that are true) As the [S] is increased, vo approaches the limiting value, Vmax KM = Vmax/2 The rate of product formed, vo, is at Vmax when [S] <<< KM KM and Vmax assist in finding the rate of the enzyme catalyzed reaction only if the reaction is considered irreversible.

Its not 0.67, 0.167, or 0.25.

Some enzymes have catalytic activity only limited by diffusion. Which rate constants of an enzyme- catalyzed reaction is/are rate limiting for the enzyme? How does this line up/compare to the rate limiting step of Michaelis-Menten Enzyme Kinetics? (Please show work and correct answer)

During a test of kinetics of an enzyme-catalyzed reaction, the following data were recorded: a. Determine the Michaelis-Menten constant for the reaction with no inhibitor present at 30 °C and at 49.6 °C. b. Determine the maximum velocity of the uninhibited reaction at 30 °C and an enzyme concentration of 1.6 g/L. c. Determine the Ki for the inhibitor at 30 °C and decide what type of inhibitor is being used.

Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?