ACTIVITY 10.8.21. Draw a schematic diagram on glycogenolysis byshowing the structural formula of its substrate. Show theenzyme required in each step2. How is glycogenolysis being regulated?

Glycogenolysis is the breakdown of the molecule glycogen into glucose, a simple sugar that the body…

Answered: 1. Draw a schematic diagram on…

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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Explain how epinephrine can serve as both a neurotransmitter and a hormone without "crossover."
2C. A “pulse-chase" experiment using "C-labeled glucose can be carried out on a yeast extract that is maintained under strictly anaerobic conditions. The experiment consists of incubating a small amount of "C-labeled substrate (the pulse) with the yeast extract just long enough for each intermediate in the fermentation pathway to become labeled. The label is then “chased" through the pathway by the addition of excess unlabeled glucose. The chase effectively prevents any further entry of labeled glucose into the pathway. 2 ADP 2 ATP Glucose ---> CH3 2 NAD* 2 NADH 2 Pyruvate H H H-C-OH C=0 CH3 CH3 2 co, 2 Ethanol 2 Acetylaldehyde (1) If [1-"C]glucose (glucose labeled at C-1 with "C) is used as a substrate, will there be any "C in the product (ii) Lactic acid is the final fermentation product in vertebrates, while ethanol is the final fermentation product in yeast. Lactic acid can be converted back into glucose while ethanol can not be. In the space below, use a thermodynamic rationale to…
1. Pepsinogen (an inactive form of the enzyme) that forms in the main cells of the stomach has a molecular weight of 42,000 D. In the gastric juice, the pepsinogen turns into the active enzyme pepsin, while its molecular weight decreases to 35,000 D. Explain the mechanism of regulation of enzyme activity. To do this: a) draw a scheme for regulating the activation of pepsin; b) name the class of the enzyme that converts pepsinogen to pepsin; c) indicate which levels of protein structural organization change when pepsin is activated.
11. Refer to the figure below. нн Н `NH2 NH2 N' N- 2e-+H* R NAD+ NADH NAD+ functions as a coenzyme in many enzyme-catalyzed reactions. The changes that take place in this coenzyme are the same for all of these reactions and are illustrated in the figure. It is likely that, in these reactions, NAD+ functions as an electron acceptor (reducing agent) in redox reactions. functions as an electron donor (oxidizing agent) in redox reactions. functions as a base in acid-base catalytic mechanisms. functions as an electron donor (oxidizing agent) in redox reactions. functions as an electron acceptor (oxidizing agent) in redox reactions. +Z-
Sketch a graph showing how the concentration of product P varies with time for chymotrypsin-catalysed hydrolysis using a substrate that displays both Michaelis-Menten kinetics and burst kinetics. On the same graph show the effect of doubling the enzyme concentration, keeping all other conditions the same.
15. The second high energy intermediate metabolite of glycolysis that can be used for substrate level phosphorylation is also a precursor molecule for the synthesis of several amino acids. Name 5 of these amino acids.
3. The reaction shown below is catalyzed along the pathway of glycolysis by an enzyme with the active site architecture shown. A. The enzyme has two Mg2+ ions, a lysine general base (deprotonated) and a glutamate general acid. In the box below, draw a plausible mechanism for this reaction, which has two formal steps with one intermediate between them (hint: one step uses the general acid and the other uses the general base.) O +(87 -00 11 R-00 00 00 + H₂O OH O Mg2+ Mg2+ Lys (general base) NH₂ OH Glu (general acid) enzyme active site
28. Sucrose in human nutrition is hydrolyzed into its monosaccharide components by sucrase. Glucose can enter directly in cellular respiration while fructose is predominantly metabolized in the liver as illustrated in the figure below. Suppose 180 molecules of sucrose are to be catabolized, what is the net ATP production during glycolysis considering both substrate-level phosphorylation and oxidative phosphorylation of NADH shuttled by malate and aspartate to the mitochondrion? [Hint: Sum of net ATP yield in substrate-level phosphorylation and ATP from glycolytic NADH] Fructose Glucose Glycogen ATP- ATP- ADP4 ADP+ hexokinase glucokinase Glucose-6-P→→→→→ Glucose-1-P Fructose-6-P Fructose-1,6-BP fructokinase rapid Fructose-1-P Rate aldolase B limiting Dihydroxyacetone-P Glyceraldehyde ATP- triose kinase ADP Glyceraldehyde-3-P Liver Also intestinal cells and kidney cortex O a. 810 ATP O b. 1260 ATP O c. 1800 ATP d. 2520 ATP PFK-1 Dihydroxy- acetone-P Lactate F1,6bisphosphatase…
19. What is the optimal pH for catalase? Why do you think it becomes less effective at high or low pH? 20. Can you think of anywhere in the human body where enzymes would work BEST at a high pH? Please give an example and draw what that graph might look like. 21. What is the optimal temperature for catalase? Why do you think it becomes less effective at high or low temperatures? 22. Can you think of any organisms that would have enzymes specifically adapted to extreme low or high temperatures and would therefore function best at a different part of the graph? Please give an example and draw what that graph might look like.
7. During amino acid catabolism, how is amino group removed and excreted in the form of urea? Please write the reactions starting from a generic amino acid to the formation of urea. Please indicate the names of enzymes, cofactors, names of substrates, and products of each reaction and the location of the reaction i.e. whether in cytoplasm or mitochondria.
1. Which of the following statements is/are TRUE for both the concerted and sequential models of allosteric enzymes? a. follows the induced-fit model b. the activator can only bind to the R form c. the inhibitor can only bind to the T form d. the substrate can only bind to the R form 2. Which of the following describes the efficiency of enzymatic catalysis? a. [S] b. KM c. Vmax d. kcat
38. The shown reaction is one of the four repeating steps during fatty acid biosynthesis. Which of the following statements is correct? 유 CH3-C-CH₂-C-S-ACP A B OH 유 CH3-C-CH₂-C-5-ACP → A. The small molecule in box A is NADPH + H* B. It is the second reduction reaction during fatty acid biosynthesis C. Both A and B D. Neither A nor B

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1. Draw a schematic diagram on glycogenolysis by showing the structural formula of its substrate. Show the enzyme required in each step 2. How is glycogenolysis being regulated?