YA*H23. Write free energy change (AG), standard free energy change (AG), and biochemical free energychange conditions (AG") (leave blank if something doesn't apply to the condition)TemperaturePressureReactant's initial conc.[H+] conc.[H₂O]Free energy change standard free energy(AG)change (AG")Biochemical standardfree energy change(AGI)

Free energy change () is the change in Gibbs free energy at any instant under consideration. The…

Answered: 23. Write free energy change (AG),…

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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111 The Michaelis constant is represented by what variable, and is comprised of which rate constants in the overall enzyme rate equation? e. Km, kf, kr and k_cat f. Vmax, kf and kcat g. Km, kf, kr and kcat h. Vmax, kf, kr and kcat Km, kf and kcat i.
b. Show calculations for making 10 mls each of the following dilutions of sucrose from the 0.30 M stock solution (Formula #3, Example D) CSTOCK (M) VSTOCK CDESIRED (M) V. X %3D X DESIRED -- . TI 0.30 M 0.25 M 0.20 M 0.15 М
Choose the correct effect. * increase decrease not change Raising the temperature slightly will... the rate of reaction Boiling temperature will... the rate of reaction Changing the pH toward the optimal pH will... the rate of reaction Introducing a competitive inhibitor will... the rate of reaction
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
Label the following equation. The parentheses represent the choices for each label (A-D). A. (Water, glucose, Carbon dioxide, Oxygen). B. (Water, glucose, Carbon dioxide, Oxygen) C. (Water, glucose, Carbon dioxide, Oxygen) D. (Water, glucose, Carbon dioxide, Oxygen)
V 23. The graph below is a graph of Vmax (a) Label the graph clearly with both the Vmax and the Km. Estimate the Km from this graph giving the correct units. v/Vmax 1.0 0.5 0.0 0.0 vs [S] for an enzyme. Enzyme Activity vs [Substrate] :0.2 0.4 Substrate (HM): 0.6 (b) If the Vmax = 25 mmoles per minute per µmole of enzyme calculate the Keat and the specificity constant."
What kind of catalysis is cysteine driving in this picture? S Los i fy R……—NHR N-H---S O. N-H H-N H-N. O Metal catalysis Covalent catalysis Base catalysis O Acid catalysis NHR²
4. Using a fluorescent model substrate, you study the kinetics of an enzyme-catalyzed reaction. You observe the below data. Write an equation describing reaction velocity (v) versus [S]. Define and provide a numerical value for any constants that you include in your equation. 16 14 12 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 [S] / mM `N' at 50 mM and observe the following In pilot experiments, you add the putative inhibitor imidazole Doesn't affect anything 1 reaction velocities: [S] = 1 mM5 µM min-1 [S] = 2 mM9 9 µM min-1 [S] = 4 mM 911 µM min-1 Is imidazole a competitive or non-competitive inhibitor? Provide a brief explanation. > 9 00 v/ µM min-
1. The concentration of substrate X is high. What happens to the rate of the enzyme-catalyzed reaction if the concentration of substrate X is reduced? Explain. 2. An enzyme has an optimum pH of 7.2. What is most likely to happen to the activity of the enzyme if the pH drops to 6.2? Explain
12. Explain why those biological reactions that have their equilibria shifted towards theproducts have negative values for ΔGo of reactions. Explain how equilibria relates toGibbs free energy.
Answer #2

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