oxidized coenzyme
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Q: Consider 3 molecules of galactose: (write only the whole number; no decimal places) a. How many…
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Q: In the citric acid cycle, malate dehydrogenase catalyzes the following reaction: Malate +…
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1. Identify the oxidized coenzyme (letter abbreviation only) that participates in this reaction of the Kreb’s cycle.
Succinate --> Fumarate
2. How many mol of NADH can be obtained upon the beta oxidation of stearic acid?
3. How many mol of ATP can be obtained upon the complete oxidation of 1 mol stearic acid?
4. How many steps in glycolysis in which ATO is converted to ADP?
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Solved in 2 steps
- Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?Complete oxidation of a 16-carbon fatty acid can yield 129 molecules of ATP Study Figure 19.2 and determine how many ATP molecules would be generated if a 16-carbon fatly acid were metabolized solely by the TCA cycle, in the form of S acetyl-CoA molecules.Based on your knowledge of the structure of NAD+ and an assumption that coenzyme dissociation is the rate limiting step of the alcohol dehydrogenase mechanism, hypothesize why a N249W mutation at the coenzyme binding site would increase the rate of catalysis.
- CHOOSE THE CORRECT LETTER 1.What kind of reaction is catalyzed by hexokinase?A. oxidationB. reductionC. phosphorylationD. isomerization 2.Which of the following reaction types are NOT found in glycolysis?A. phosphorylationB. reductionC. oxidationD. isomerization 3.What type of reaction is catalyzed by glyceraldehyde-3-phosphate dehydrogenase?A.phosphorylationB.reductionC. isomerizationD. oxidationasap2. Lactate dehydrogenase (LDH) catalyzes the reaction Ο ()) 0 NADH + H* NAD+ C=0 HO-C-H CH₁t Pyruvate lactate dehydrogenase CHa L-Lactate AG 25.1 kJ/mol which represents one of the metabolic fates of pyruvate, the end product of glycolysis. The positioning of the sub-strate pyruvate in the active site of lactate dehydrogenase is shown on the right. NADH (nicotinamide adenine dinu- cleotide) is a cofactor in the reaction and provides a hydride anion H (highlighted with light blue) through direct transfer to reduce the carbonyl group of pyruvate. (a) ( Gln 102 Arg109 NH2 NH Thr246 H₂C-C-OH HN NH H CHS H H H. His 195 NH Pyruvate N-(NADH) H H CH3 H HN H NH H₂C-C-CH₂ Пle250 Asp168 NH Arg171 ) Compare the mechanism of the LDH reaction, as implied by the diagram above, to that of a-chymotrypsin with respect to the oxyanion hole, conversion of the substrate carbonyl group having sp² hybridization to sp³ hybridization, the attacking nucleophile, and residues achoring the substrate in the active…
- CHOOSE THE CORRECT LETTER 1.Which of the following enzymes need ATP as a substrate in the reaction?A.phosphoglycerate kinaseB. phosphofructokinaseC. pyruvate kinaseD.glyceraldehyde-3-phosphate dehydrogenase6. Malate dehydrogenase catalyzes the following reversible reaction: COO- HO-C-H CH₂ COO™ L-Malate NAD+ y malate NADH + H+ dehydrogenase COO- 0=C CH₂ COO™ Oxaloacetate AG'° = 29.7 kJ/mol Malate + NAD+→NADH + H+ + oxaloacetate Calculate AG" and the ratio or products and reactants for the malate dehydrogenase reaction to proceed from left to right as shown. (The Faraday constant. 3, is 96.48 kJ/V-mol; RT(37°C)= 2.58kJ/mol) Steps: 1. Explain how you determined which molecule is an electron donor Malate and which is an acceptor NAD*. -2- 2. Calculate AED (write equation, then show calculations, for standard reduction potentials (E_values) see table in the posted lecture) 3. Calculate AG (write equation, then show calculations) 4. Calculate the ratio of products and reactants needed to for Malate + NAD+→→NADH + H+ + oxaloacetate reaction to proceed forward (write equation, then show calculations)3.) As mentioned in the March1 outline a critical step in the glycolysis metabolic pathway (conversion for glucose to pyruvate that produces 2 ATP's) is the attachment of dihydroxyacetone phosphate to an isomerase enzyme via an iminium bridge (step1). There is a second step that takes the imine to the enamine that sets up the C-C formation reaction with an enol that you'll cover in two weeks. Show the mechanism for steps 1 (mild acid catalysis) and 2 (draw resonance forms for the iminium cation). In your mechanism, show the intermediate hemiaminal (carbinolamine). Step 2 may address one of the questions asked in Wednesday's class about the water taking out the N-H proton of the iminium cation versus a C-H proton? CH₂OPO3² E-NH₂ + O=C (step 1) CH₂OH Dihydroxyacetone phosphate Iminium (+) cation intermediate (step 2) Enamine (Enol) Intermediate H CH₂OPO32- E-N-C H C. OH H₂O E
- Citrate (the product of the first step of the TCA cycle) is considered to be a sign of high energy. 1. Which step of glycolysis does citrate regulate (does it activate or inhibit that step?) 2. WHY exactly is citrate considered a sign of high energy?Given the following question on the image identify the following:1. Total number of glucose molecules entering glycolysis2. Total number of pyruvate molecules produces at the end of glycolysis3. Total number of mitochondrial NADH produced after pyruvate is acted upon pyruvate dehydrogenase complex4.Total number of CO2 released right after the pyruvate dehydrogenase complex reactionConsider that the shuttle system is maltase-aspartate shuttleConsider 3 molecules of galactose: (write only the whole number; no decimal places) How many turns of Krebs Cycle will these molecules undergo for complete oxidation? b. How many moles of ATP are produced upon complete oxidation via malate-aspartate shuttle? c. If all the galactose molecules oxidize via pentose phosphate pathway (oxidative stage only), how many moles of NADPH will be produced?