(a)
Interpretation:
The results obtained with the mutant should be explained.
Concept introduction:
Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen
(b)
Interpretation:
The effect of substituting aspartic acid for serine should be predicted.
Concept introduction:
Glycogen phosphorylase catalyzes the cleavage of the terminal alpha-1,4-glycosidic bond of glycogen polymer releasing glucose-1-phosphate. The most important regulatory site in glycogen phosphorylase is Serine 14 residue. Phosphorylation of this ser-14 residue activate phosphorylase b form to phosphorylase a form.
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Chapter 21 Solutions
BIOCHEMISTRY
- In full details. Define 'activation energy' of an enzyme catalysed single substrate reaction and mention the effects of an enzyme on this energy.arrow_forwardThe Cori Cycle. Before vigorous exercise (at rest) the level of blood lactate is at its normal level (about 25 mM). During a 400 m sprint, the value rises sharply in less than a few minutes to about 200 mM and then declines slowly to around 40 mM over 60 mins after the sprint. a. Discuss (or illustrate) the pathway and reactions that cause the rapid increase in lactate concentration during the sprint. b. What causes the slow decline in lactate concentration after the sprint? Why does the decrease occur more slowly than the rapid increase? c. What enzymatic reaction is responsible for maintaining the lactate concentration above zero at recovery after the sprint?arrow_forwarddisease. As such, a frontline treatment for Type 2 diabetes is the drug metformin, which acts indirectly to inhibit gluconeogenesis in the liver. You are a research biochemist who would like to develop new drugs that act to directly inhibit gluconeogenesis. You have just gained access to a library of thousands of small molecules of unknown activity, and you would like to identify lead compounds that have specific inhibitory activity against steps in the gluconeogenesis pathway. (a) into PEP in order to screen for inhibitors of enzymes specific to gluconeogenesis. Which enzymes do you need to purify, what cofactors and allosteric effectors do they require, and which reactants do you need to add to reconstitute the reactions for the first bypass? Which intermediates and products are generated? Your first approach is to reconstitute the initial set of bypass reactions that convert pyruvate (b) vitro reconstitution? What additional steps and enzymes are required in liver cells but are…arrow_forward
- Anser in your own words. a. During pregnancy, do mother and child share the same blood? What if they have different blood types? b. If a patient takes a large dose of a drug that blocks calcium channels, what happens to the heart? c. The enzymes of the digestive system are classified as hydrolases. What does this mean? d. Explain in a scientific but simple manner the idiomatic expression “butterflies in my stomach”.arrow_forwardFill in the blanks.: Write Cif 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 enzyme catalyzes a reaction by providing an alternative reaction pathway that has a lower energy of activation. B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to the uncatalyzed reaction.arrow_forward. Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reactionarrow_forward
- - Keto counterparts. Name the a-ketoacida-ketoacid that is formed by the transamination of each of the following amino acids: Co, a. Alanine b. Leucine c. Aspartate d. Phenylalanine e. Glutamate f. Tyrosinearrow_forwardOH affromah. The Standard free energy CAGO¹) of the reaction shown above can be estimated based on? OH A. High Energy bands B. Reduction potential C. cannot be estimated OH energy. он The reaction shown above requires the cofactor to proceed forward without significant was te of A.ATP B. Nicotinamide C. Flavin D. No cofactor required 3 Determine approximate 46°1 of the coupled reaction KJ/mol possible answers: (0,-8,-15,-22,-30, -38,-45) The class of enzyme that catalyzes the reaction is possible answers: Mutase, Isomerase, ki nase, phosphatase, Dehydrogenase, Aidolasearrow_forwardX INCORRECT; see section 13.1 Enzymes occasionally display weak "“side" activities. Draw the structure of the product (other than ADP) of the reaction that results when pyruvate kinase, operating in reverse, uses lactate as a substrate. For your structure: 1. Do not include primary or secondary hydrogens. CH2 HO OH Edit Drawingarrow_forward
- Draw Gluconeogenesis. Please make sure to state all the enzymes and co-factors for each step of the pathway. note you are responsible for all the enzymes for each step, even though it is not stated on the slide.arrow_forwardelearn.squ.edu.om/mod/qui ystem (Academic) The enzyme asparaginase is used to reduce the level of asparagine in blood in the treatment of leukemia. Which of the following forms of Asparaginase would be most useful if the blood asparagine level is 0.2 mM? Select one: O a. Km = 2.0 mM; Vmax = 0.1 mM/hour O b. Km = 0.1 mM; Vmax = 0.5 mM/hour %3D О с. Кm 0.2 mM; Vmax = 0.1 mM/hour O d. Km = 0.1 mM; Vmax = 0.1 mM/hour O e. Km = 0.2 mM; Vmax = 0.5 mM/hour Clear my choice In a steady state (of ES formation and ES breakdown) Select one: a The rate of formation of ES is equal to the rate of its degradation during the reactionarrow_forwardJust Arrange. The enzyme serine hydroxymethyltransferase (SHMT) requires pyridoxal phosphate (PLP) as a cofactor. Arrange the steps of the likely mechanism for SHMT‑catalyzed serine degradation (producing glycine and N5,N10‑methylenetetrahydrofolate)arrow_forward
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