Michaelis-Menten kinetics are used to describe intracellular reactions. Yet [Eo] [So]. In in vitro batch reactors, the quasi-steady-state hypothesis does not hold for [Es] [So]. Similarly, the rapid equilibrium assumption also will not hold. Rationalize why Michaelis-Menten Kinetics and the quasi-steady-state approximation are still reasonable descriptions of intracellular enzyme reactions.

Michaelis-Menten kinetics are used to describe intracellular reactions. Yet [Eo] [So]. In in vitro batch reactors, the quasi-steady-state hypothesis does not hold for [Es] [So]. Similarly, the rapid equilibrium assumption also will not hold. Rationalize why Michaelis-Menten Kinetics and the quasi-steady-state approximation are still reasonable descriptions of intracellular enzyme reactions.

Principles of Modern Chemistry

8th Edition

ISBN:9781305079113

Author:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler

Publisher:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler

Chapter18: Chemical Kinetics

Section: Chapter Questions

Problem 75AP

See similar textbooks

Similar questions

When studying the inhibition kinetics of a certain enzyme, the results have been obtained from the following table: Determine graphically:a) the type of inhibition b) the KM value of the enzyme c) the maximum speed of this experiment d) the value of Ki.
An enzyme kinetics experiment is carried out by adding 1.00mg of a 50.0kDa enzyme into a total volume of 50uL of buffer, and measuring the initial rates while adding increasing amounts of substrate (1 Da = 1 g/mol). The calculated Vmax from this series of experiments was 30.5mM/s. Calculate the turnover number for the enzyme.
The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8
Plot the following information using both the michaellis-Menten and Lineweaver-Burt plots. (Assume enzyme concentrationis constant)
Give the Vmax and Km for this enzyme that obeys Michaelis-Menten kinetics. Use 2 sig figs.
Discuss the assumptions made when deriving the Michaelis-Menten model of enzyme kinetics.
How many kJ/mol must an enzyme lower the activation energy of the reaction to make it useful? We known that in the absence of a catalyst a certain biochemical reaction occurs x times per second at normal body temperature which is 37 degrees C. The reaction needs to occur 5000 times faster than when it's uncaralyzed in order to be physiological useful. For this problem use the Arrhenius expression for the rate constant k to derive the equation for deltaEa under constant temperature.
An enzyme with a single active site has a Michaelis-Mentin constant (KM ) of 25 mM and aturnover number of 4.0 x 107 s –1 .(a) Calculate the initial rate of the reaction in μM/s if the total enzyme concentration is0.016 μM and the initial substrate concentration is 4.32 μM.(b) Calculate the value of Rmax
Determine the value of the turnover number of the enzyme catalase, given that RmaxRmax (Vmax)(Vmax) for catalase is 41 mmol⋅L−1⋅s−141 mmol⋅L−1⋅s−1 and [E]t[E]t equals 4.8 nmol⋅L−14.8 nmol⋅L−1 . Catalase has a single active site.
what is the approximation used to derive the reaction rate for an enzyme catalysed reaction that proceeds by a michaelis menten mechansim
Kinetic assays were performed to better understand the activity of the enzyme 245C in the absense and presence of molecule B. The enzyme follows Michaelis-Menten kinetics. a) Calculate the VO for this enzyme when [S]=0.03mM and no molecule B is present. b) Using a properly labelled Lineweaver-Burke plot with accurate x- and y-intercepts, describe the effect of molecule B on the enzyme. Briefly explain how molecule B could be causing these effects.
Salicylic acid salts inhibit the catalytic action of a glutamate dehydrogenase. Determine the type of inhibition by graphical analysis of the Following data. Assume that the salicylate concentration remains constant and is 40 mM. Also calculate the KM for the substrate and the dissociation constant for the enzyme-inhibitor complex. [S] mM 1.5 2.0 3.0 4.0 8.0 16.0 Without salicylate Product (mmol/min) 0.21 0.25 0.28 0.33 0.44 0.4 With salicylate Product (mmol/min) 0.08 0.10 0.12 0.13 0.16 0.18