(a) V(b) V[S][E;)(e) [P]Time Sketch the appropriate plots on the following axes. Assume that simple Michaelis-Menten kinetics apply, and that the pre-steady state occurs so rapidly that it need notbe considered

Introduction Briggs and Haldane refined the Michaelis-Menten model by steady-state assumption. It…

Answered: (a) V (b) v [S] [E;] (e) [P] Time

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Derive the complete rate equation using the King altman method. Example is shown above the reaction mechanism. All the N terms must be derived.
A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 m mol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM?
Regarding the reasoning for the Michaelis-Menten equation to be unsuitable for accurate analysis of experimental data, select all that apply: It is nonlinear It is only valid for reactions at equilibrium It is not valid under experimental conditions Extrapolation to Vm is inaccurate and therefore Km also cannot be accurately described
For the following first-order liquid-phase reversible reaction, where initially only reactant A is present: k₁ AR, k2 Equilibrium constant: K 1) Express the equilibrium conversion rate, Xe, using K, and demonstrate that Xe can be determined using thermodynamic data. 2) Show how the rate constants kl and k2 can be determined experimentally.
If a data from an enzyme experiment is plotted as a Lineweaver - Burk plot, and the Vmax is 0.02 sec/mol, and x-intercept is -2.5 mM-1, then what is the KM value?
A bacterial enzyme catalyzes the hydrolysis of maltose as shown in the reaction given below: Maltose + H2O -> 2 glucose If the reaction has a Km of 0.135 mM and a V max of 65 umol/min. What is the reaction velocity when the concentration of maltose is 1.0 mM? (Please take note of the units)
Consider the following reaction:ATP → AMP + 2 PiCalculate the equilibrium constant (Keq) given the following ΔG°′ values:ATP → AMP + PPi (−32.2 kJ/mol)PPi → 2Pi (−33.5 kJ/mol)
The table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.
For a particular reaction, AH° = −16.1 kJ/mol and AS° = −21.8 J/(mol·K). Assuming these values change very little with temperature, at what temperature does the reaction change from nonspontaneous to spontaneous in the forward direction? OT= Is the reaction in the forward direction spontaneous at temperatures greater than or less than the calculated temperature? less than greater than K
What are the benefits of measuring the initial rate of a reaction Vå for use in kinetic studies? (This is a multi-select question). [ES] can be measured accurately. changes in [S] are negligible, so the value of [S] is known. changes in Km are negligible, so Km can be treated as a constant. V₁ = Vmax. --> A negligible amount of product has formed, so that the back reaction P -- need not be considered. ES
How is this equation derived? from pre-existing michaelis menten kinetics assumptions?
Answer the following questions yes or no (Y/N): Is the michaelis-menten equation valid under experimental conditions? Is the michaelis-menten equation only valid for reactions that are at equilibrium? Is extrapolation to Vm inaccurate, but Km is accurately determined in the michaelis-menten equation? Is the michaelis-menten equation nonlinear? Is extrapolation to Vm inaccurate, and therefore Km cannot be accurately determined in the michaelis-menten equation?

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