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- Question 1. Put away your notes and text and draw the complete Calvin-Benson cycle starting from 3molecules of Ru1,5BP. Show stoichiometry along the way using 6 GAP molecules to regeneratethe 3 Ru1,5BPs. Label each reaction according to its enzyme class (your choices arecarboxylase, kinase, dehydrogenase, aldolase, epimerase, isomerase, phosphatase, andtransketolase – see the posted enzyme guide for help on this).QUESTION 10 Which one of the following statements does NOT correctly describe the current state of the chymotrypsin-substrate complex below or the next mechanistic step that occurs? s,' G193 S195 NH NH R -NH R-NH HN- Ser-195 His-57 HN Asp-102 OA. This intermediate is part of a nucleophilic acyl substitution reaction. OB. In the next step His-57 protonates Ser-195. O C. In the next step His-57 activates a water molecule. O D. In the next step His-57 protonates the leaving group. OE. In the next step the N-terminal fragment of the original substrate departs.Question 1. (a) The TCA cycle plays a a central role in the aerobic catabolism of fuel molecules. Explain the dependence of the TCA cycle on aerobic conditions, (b) Compute the theoretical yield of ATP by oxidative phosphorylate when the acetyl-CoA obtained from B-oxidation of palmitic acid (16:0) is completely in an e aerobic cell show all working.
- Question 9 If 14CO2 (radioactive carbon) were incorporated into the TCA cycle via the Pyruvate Carboxylase reaction which of the following molecules would contain radioactive carbon? O Multiple answers: Multiple answers are accepted for this question Select one or more answers and submit. For keyboard navigation. SHOW MORE V a Oxaloacetate b Citric acid Isocitric acid d a-Ketoglutarate e Succinyl-CoA f Succinate Fumarate h MalateQuestion 2. An enzyme was found to convert Acetyl-coA to an acetyl-cysteine intermediate of the enzyme. The structure of cOA is: H H НО СН; HS — СH2— СH2 — N—C—CH,— CH2—N- С—С—С—CH;—0—Р- 0–CH2 Adenine н CH H H H Phosphopantetheine group of coenzyme A 2-O3PO ОН Draw a plausible chemical mechanism. Where is the acetyl-group in acetyl-coA? What is the reactive group of the protein? The reaction is enhanced at higher pH. How is this consistent with your mechanism? Is covalent catalysis involved?Question 1. Answer the following questions: A. The complete oxidation of 1 mole of glucose to CO2 and H2O yields 686 kcal of free energy.How many ATP molecules could maximally be generated from one molecule of glucose, if theuseful chemical energy available in the high energy phosphate bond of 1 mole of ATP is 12kcal? B. However, it is known that cellular respiration produces 30 moles of ATP from 1 mole ofglucose. How does this compare with your answer in part (A)? Estimate the overall efficiency ofATP production from glucose? C. Assume that the cells of your body are oxidizing glucose and no energy is being dissipated asheat to the environment. However, the heat not converted into chemical-bond energy isincreasing the temperature of your body. How much would the temperature of your body riseupon oxidation of 1 mole of glucose if your body consists of 75 kg of water. [Hint: One kilocalorie (kcal) is defined as that amount of energy that heats 1 kg of water by 1oC]
- QUESTION 34 Which of the following represents a reaction that could be used to refil the TCA cycle Aspartate -a -ketoglutarate Pyruvate Oxaloacetate O Oxaloacetate- Phosphoenol pyruvate Citrate - Oxaloacetate + acetyl COAQuestion 2. Answer the following questions: A. The following experimental data was collected during a study of the catalytic activity of anintestinal peptidase with the substrate glycylglycine. Plot the data as a graph, and use it toestimate the Km and the Vmax for this enzyme. B. Now transform this data to plot it as a straight line (Lineweaver-Burk plot). Determine Km andthe Vmax for this enzyme using this new plot. Do your results agree with the estimates made fromthe first graph of the raw data (from 2A)? C. Now assume that the activity of this intestinal peptidase is regulated by covalent modificationof its catalytically active amino acid. Upon phosphorylation, the Km of the catalyzed reaction has been observed to increase by a factor of 3 without any effect on its Vmax. Is the enzyme getting activated or inhibited upon phosphorylation? Justify your answer. D. How will the Lineweaver-Burk plot of the phosphorylated enzyme differ from the plot of the unmodified enzyme (from 2B)?…QUESTION 13 The beta-oxidation pathway consumes fatty acyl-CoAs, generating oxidized cofactors and CoA consumes fatty acyl-CoAs, generating FADH2, NADH, and acetyl CoAs consumes fatty acyl-CoAs, generating FAD, NAD*, and acetyl COAS generates fatty acyl-CoA, FADH2, NAD*, and acetyl CoAs O consumes fatty acyl-CoAs, generating FAD, NADH, and CO2
- 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 7 of 16 ©Mat One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. W F2 #m 3 E How many molecules of fumarate can one molecule of fumarase act on in 29.0 min? D fumarate Lactate dehydrogenase lactate fumarate molecules: F3 > Enzyme Ribonuclease Fumarase $ 4 R Urease F F4 % 5 T G B 6 HOLO F5 Substrate Turnover number (per second) RNA 100 800 1000 10.000 Y H & 7 urca F6 U J DELL * 8 CO F7 K ( 9 FB O P ; man Wi F10 [ F11 1 F12 Backspace Enter Insert Print Screen Shift Delete Home Scroll Lock Answer End 8:24 PM 10/15/2023 + PgUp Pause Break PgDn Num Lock 7 Home 4 1 EncQUESTION 3 Biocatalysts are effective because: O a. They increase the activation energy of a reaction Ob. They stabilize the transition state O. They decrease the rate of the reaction Od. They decrease the activation energy of a reaction QUESTION 4 Which of the following statements is INCORRECT regarding L-amino acids and D-amino acids? O NH3 group on the left of the chiral carbon in both isomers O b. They are nonsuperimposable mirror images of each other O NH group on the left of chiral carbon in L isomers Od. They are enantiomers