Consider the two reactions below. They are fast and have reached equilibrium by the end ofthe time shown. At time zero (t = 0) which is true?[Product] (M)I21TimeThe AG of reaction 1 is greater (more positive) than the AG of reaction 2.The AG of reaction 1 is less (more negative) than the AG of reaction 2.○ The AG of reaction 1 is equal to the AG of reaction 2.

Reaction 1 (blue curve): Starts at a high product concentration and decreases to a lower equilibrium…

Answered: Consider the two reactions below. They…

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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The enzyme triosephosphate isomerase (TIM) catalyzes the following reaction in glycolysis, where it converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (GAP). CH₂OH C=O CH₂OPO²- DHAP triose phosphate isomerase [DHAP] (MM 1.00 2.00 3.00 6.00 O V. (mM/s) 3.700 6.727 9.250 14.800 = H HCOH CH₂OPO²- Kinetics experiments were performed on TIM. Enzyme activity (initial velocity, V.) was measured at varying concentrations of DHAP. The enzyme kinetics were also measured in the presence of two inhibitors, A and B. The enzyme concentration used in all experiments was 25.00 μM. The data are shown below. GAP V. (mM/s) + A 1.452 2.794 4.038 7.281 V₁ (mM/s) + B 0.755 1.379 1.905 3.077
What is the Keq of Reaction #3? Show your work & clearly label your answer. Is Reaction #3 favorable under mammalian cellular conditions when the concentration of dGTP is 0.2 M, dCMP is 20 mM, dGMP-dCMP is 7 mM, and PPi is 10 mM? Use △G to support your answer.
Which rate law has a molecularity of zero? Select one: O a. Rate = k[A]° O b. Rate = k[A][B] %3D O c. Rate = k[A][B][C] %3D O d. Rate k[A] %3D K[AJ? e. Rate = Determine the value of K. for the following reaction if the equilibriu
What is △Go of Reaction #3? What is the Keq of Reaction #3? Show your steps please
An enzyme catalyzes a reaction with a Km of 7.50 mM and a Vmax of 2.90 mM - s-1. Calculate the reaction velocity, un, for each substrate concentration. [S] = 2.75 mM mM · s- * TOOLS x10 [S] = 7.50 mM mM · s-! [S] = 11.0 mM mM - s-
When the following equation of a redox reaction in acidic solution is properly balanced, what are the coefficients for Cr2O72–, Fe2+ H+, Cr3+, Fe3+, and H2O, respectively? __Cr2O72– + __Fe2+ + __H+ --> __Cr3+ + __Fe3+ + __H2O (A) 1, 3, 14, 2, 3, 7; (B) 1, 6, 14, 2, 6, 7; (C) 2, 10, 14, 2, 10, 7; (D) 2, 12, 28, 4, 12, 14
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Given the initial rate data for the reaction A + B → C, determine the rate expression for the reaction. [A], M [B], M A[C]/At (initial) M/s 0.0418 0.122 2.73 x 10-4 0.0836 0.122 10.9 × 10 4 0.0418 0.488 2.73 x 104 O A[C] At ○ A[C] ΔΙ = 0.439 Ms[A][B]² = 1.27 M²s¹ [A][B] ● A[C] = 6.53 × 10³ s¹ [A] At O A[C] = 0.156 M's¹[A]² At ○ A[C] At = 5.35 x 102 M2s[A][B]
None
5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
make a Gibbs free energy graph as free energy as y-axis a for the transition state as a function of [Gdn HCl] (x-axis) with a line of best fit

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