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
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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-
While furthering your studies of iocane powder you determine that a ceular enzyme, iocase will degrade it. Under normal conditions, iocase shows km 0f 1.85 uM and a kcat of 76. The drug sildenafil was found to have no effect on the km of iocanse yet the kcat was found to drop 58 minutes^-1, when the drug was added and no other changes were made in the reaction conditions. What can be inferred from this data? (remember kcat = vmax/et) Sildenafil acts as an uncompetitive inhibitor of iocanse Sildenafil acts as a noncompetitive inhibitor of iocanse The effect of sildenafil could be countered by adding more iocane to the reaction The y-intercept of the sildenafil inhibited iocanse would appear to be lower on a Lineweaver burke plot as compared to uninhibited iocanase The slope of a Lineweaver burke plot of the inhibited versus uninhibited iocanase would remain unchanged
For the following reaction X + YA + B at 300 K, it is found equilibrium constant equal to 10. Therefore, AG & AGⓇ of the reaction at 300 K respectively are - Answer b
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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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3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: |[S), mM 0.050 0.075 v, (µM min") 0.93 1.264 1.77 2.14 3.7 0.125 0.175 0.935 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme d. The same reactions are performed in presence of an inhibitor A and the resulting velocities determined: v plus inhibitor, (µM min) 0.272 0.37 0.518 0.626 |1.08 |[S), mM 0.050 0.075 0.125 0.175 0.935 Plot these data on the same graph as above and determine the new Km and Vmax and the type of inhibitor (competitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?
The decomposition reaction of hydrogen peroxide (H₂O₂) proceeds as follows: 2 H₂0₂ → 2 H₂O + 0₂ 2 This reaction can occur without a catalyst, in the presence of a chemical catalyst (platinum) or of a biological catalyst (catalase). 1- From the values given in the table below, determine the catalytic power of each catalyst (ratio of the catalyzed rate of reaction to the uncatalyzed rate). 2- Which catalyst is the most efficient? Reaction conditions No catalyst Platinum Catalase Ea (kJ.mol¹) at 20 °C 75 49 8

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