At 300 K, what fold improvement in a reaction rate do you expect if AG* is brought down from 40 kJ/mol to 20 kJ/mol, without changing of the reaction mechanism, as a result of enzymatic catalysis? е. f. The following may or may not be affected by the addition of an enzyme to a chemical reaction. State if there will be (1) no effect, (2) an increase, or (3) a decrease? A) activation energy of the reaction B) standard free energy of the reaction C) time to reach equilibrium D) equilibrium constant of the reaction E) initial velocity of the reaction g. Remember the simple kinetic mechanism for an enzyme-catalyzed reaction. It was reported that the rate-limiting step is the following reaction ES > P Under these circumstances, the Michaelis constant becomes equivalent to A) [S], when Vo = Vmax B) Turnover number C) Specificity constant D) kcat E) the dissociation constant for the Enzyme-Substrate (ES) complex

At 300 K, what fold improvement in a reaction rate do you expect if AG* is brought down from 40 kJ/mol to 20 kJ/mol, without changing of the reaction mechanism, as a result of enzymatic catalysis? е. f. The following may or may not be affected by the addition of an enzyme to a chemical reaction. State if there will be (1) no effect, (2) an increase, or (3) a decrease? A) activation energy of the reaction B) standard free energy of the reaction C) time to reach equilibrium D) equilibrium constant of the reaction E) initial velocity of the reaction g. Remember the simple kinetic mechanism for an enzyme-catalyzed reaction. It was reported that the rate-limiting step is the following reaction ES > P Under these circumstances, the Michaelis constant becomes equivalent to A) [S], when Vo = Vmax B) Turnover number C) Specificity constant D) kcat E) the dissociation constant for the Enzyme-Substrate (ES) complex

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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An enzyme catalyzes a reaction at a velocity of 20 μmol/min when the concentration of substrate (S)is 0.01 M. The Km for this substrate is 1 × 10-5 M. Assuming that Michaelis-Menten kinetics arefollowed, what will the reaction velocity be when the concentration of S is 1 ×10-6 M?
At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of the uncatalyzed reaction. Assuming that the frequency factor A is the same for both reactions, by how much does the enzyme lower the Eₐ?
Based on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surely
An enzyme that follows simple Michaelis–Menten kinetics has an initial reaction velocity of 10 µmol⋅min-1 when the substrate concentration is five times greater than the KM. What is the Vmax of this enzyme in µmol⋅min−1?
The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.
An enzyme that follows Michaelis-Menten kinetics has a KM value of 10.0 μM and a kcat value of 206 s−1 . At an initial enzyme concentration of 0.0100 μM , the initial reaction velocity was found to be 1.07×10−6 μM/s . What was the initial concentration of the substrate, [S] , used in the reaction ? Express your answer in micromolar to three significant figures..
If the hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase has a ΔG′∘ of −11.386 kJ/mol at 25 °C, what percentage of substrate remains once the reaction reaches equilibrium assuming no product was initially present? (Round answer to the nearest whole number)
For an enzyme that displays Michaelis-Menton kinetics, what is thereaction velocity, V (as a percentage of V max , observed at the followingvalues?[S] = K M[S] = 0.5K M[S] = 0.1K M[S] = 2K M[S] = 10K M
An enzyme catalysed reaction has a Km of 8 mM and a Vmax of 13 nM.s-1. Use the Michaelis-Menten equation to calculate the reaction velocity when the substrate concentration is 18 mM.
The hydrolysis of ATP has an enthalpy and entropy of -24.3 kJ/mol and +21.6 J.K-1.mol-1, respectively, at 37 o C. What is the free energy change for the hydrolysis of 5 mols of ATP? Explain what contributes to the negative enthalpy change and positive entropy change in this reaction. What physical characteristics of the reaction would change if an ATP hydrolase enzyme is added to the solution?
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when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.