Question #8 Shown below are the chemical structures of several cofactors that are used in enzyme catalyzed reactions. For each, (i) provide the full name of the cofactor, (ii) indicate what it carries (e.g. both one and two electrons in H+/e- increments) and (iii) circle the specific site on the cofactor that is directly involved in catalysis. The answer for panel A is given as an example.

Question #8 Shown below are the chemical structures of several cofactors that are used in enzyme catalyzed reactions. For each, (i) provide the full name of the cofactor, (ii) indicate what it carries (e.g. both one and two electrons in H+/e- increments) and (iii) circle the specific site on the cofactor that is directly involved in catalysis. The answer for panel A is given as an example.

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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QUESTION 28 Recall the reaction catalyzed by phosphoglucomutase: glucose-1-phosphate glucose-6-phosphate Assume that in liver cells under fed conditions, the G1P concentration = 2.5x10-2 M, and the G6P concentration = 1x10-3 M. Using the equation AG = AGO + RTIN([product)/freactant]), calculate AG for the reaction, given that: AGO = -7.1 kJ mol-1 R = 8.315x10-3 kJ mol-1 K-1 T = 310 K (37°C) In which direction will the reaction proceed spontaneously under these conditions? O +1.2 kl mol1; reverse reaction spontaneous. O -3.5 kl mol-1: forward reaction spontaneous. O -10.7 k) mol1; forward reaction spontaneous. O -15.4 kJ mol1; forward reaction spontaneous.
Question 9: For the reaction catalyzed by the enzyme hexokinase, Glucose + ATP = glucose 6-phosphate + ADP, the equilibrium constant is 7.8 x 10² at 298 K. Please answer the following independent questions. A. Determine the standard Gibbs free energy of the reaction. B. In dying E. coli cells, the concentrations of metabolites were found to be: [ATP] = 0.5 mM, [ADP] = 100 mM, [glucose] =0.1 mM, and [glucose 6-phosphate] = 2 mM ay 298 K. Does the reaction proceed spontaneously? C. What would be the ATP:ADP ratio at equilibrium at 37 C if the concentration of glucose is 100- fold less than that of glucose-6-phosphate? The standard enthalpy of this reaction at 298 K is - 23.8 kJ/mol.
Question 9 Which of the following is TRUE of the branching reaction of glycogen? a) Each linear chain of glucosyl units can have a maximum of four branches attached to it. b) The branch point cannot be within six residues of a preexisting branch point. c) A chain of glucosyl units must be at least seven units long to be a substrate for the branching enzyme. d) The block of glucosyl residues transferred to form a branch is usually three residues in length. e) A chain of glucosyl units must be at least 11 units long to be a substrate for the branching enzyme.
QUESTION 24 For a simple enzyme-catalyzed reaction, double reciprocal plots were determined for three different enzyme concentrations. Which of the following plots would you expect to observe ? A) B) C) D) E) 1/v, 1/v 1/v 1/v. 1/v 1/[S] 1/[S] 1/[S] 1/[S] 1/[S] O A. A) O B. B) OC.C) O D. D) O E. E)
QUESTION 10 Select a property that does not belong to allosteric enzymes. They conform to hyperbolic Michaelis-Menten kinetics They may have binding sites for regulatory molecules that are separate from active sites They tend to have a signmoidal curve of rate versus [S] They undergo conformation changes as a result of modulator binding.
Question 6 Review Concept 8.4 Enzymes. Match the term and its description. Each term can only be used once. These are nonprotein enzyme helpers. [ Choose) These inhibitors bind to the active site of an enzyme, [ Choose ) competing with the substrate to decrease reaction > >
The following questions deal with a fundamental understanding of enzyme catalysis.a. Why is the rate of an enzyme-catalyzed reaction proportional to the amount of (ES) complex?b. What do you think is meant by saturation of the enzyme?c. What do you think is meant by the term “saturation kinetics”?d. How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reachesa maximum value at high [S]?
QUESTION 10 A) In glycolysis, the glucose which has 6 carbon molecules is eventually broken down into 2 molecules of 3 carbon compounds as pyruvate. Regardless of all the enzymes involved, describe the key points that change the 6 carbon compound into two molecules of 3 carbon compound. B) As glycolysis splits glucose into two pyruvate molecules, the link reaction occurs twice per molecule of glucose. Briefly explain the process after pyruvate transported from the cytosol into the mitochondrial matrix.
Question 9 The nucleoside monophosphates are seen in metabolic pathways because their phosphoric anhydride bonds can be hydrolyzed off for energy. A) True B) False
Question 13 of 13 Fill in the blanks: Write C if only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A.An inhibitor that binds somewhere in the enzyme other than the active site is an uncompetitive inhibitor. B. With this mode of inhibitor binding, the substrate's affinity to the enzyme is affected and it decreases the maximum reaction velocity.
Question 1: The overall process enabled by the glyoxylate cycle is: (2acetyl-CoA) + (NAD+) + (2H2O) → (succinate) + (2CoA) + (NADH) + (2H+) Dissect this process further by writing down all of the reactions that are actually involved in making one succinate from two acetyl-CoA units. Show chemical structure for all intermediates.
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