8. Compare the ATP yield for the complete oxidation of glutamate and methionine, both of which contain fi ve carbon atoms, to CO2. you can assume NADH (or NADPH) and FADH2 yield 2.5 and 1.5 ATP equivalents, respectively. The oxidation of malate is performed by malic enzyme
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8. Compare the ATP yield for the complete oxidation of glutamate and
methionine, both of which contain fi ve carbon atoms, to CO2.
you can assume NADH (or NADPH) and FADH2 yield 2.5 and 1.5 ATP
equivalents, respectively. The oxidation of malate is performed by malic enzyme
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- vat *Pyruvate carboxylase, which catalyzes conversion of pyruvate to medbo which cat oxaloacetate, is a regulatory enzyme activated by acetyl-SCOA.A ms Ido Explain why this control is advantageous to organisms. el pidotes to 316q beisbianoo olovo bios bixdio eda ei ydw ni 169qqs son esob nopyxo 16Iuselom nouods nove mellodstem Slovo od to noijose s zonado nostoals ont To 9300098 opo bias oito any contenos ain't ty dopo of basi sio S OU *While acetyl-SCOA activates pyruvate carboxylase, it inhibits pyruvate kinase. Explain how this is consistent with the idea of 9 complementary control.pе pпiwollot or to doss to slovo bios sitio :eyswdisq otlodsjem E2- noitididat xosdb99t28. 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…2. Consider a preparation that contains all of the enzymes and cofactors needed for fatty acid biosynthesis from added malonyl-CoA and acetyl- COA. a. If [2-H) acetyl-CoA (labeled with deuterium) H-c-C-COA and an excess of unlabeled malonyl-CoA are added as substrates, how many deuterium atoms are incorporated into each palmitate? What are their locations in the palmitate structure? (Draw an expanded structural formula for palmitate showing the locations of the deuterium atoms (as drawn in acetyl-CoA above). Explain your answer.
- (d) of glucose oxidation in diabetic human patients treated with Metformin (●) and in (nondiabetic) control human patients (0). At –150 min both groups of subjects were started on an intravenous feed of 3-(®H)-glucose, and at t = 0 min they were started on an oral glucose tolerance test whereby a measured amount of glucose in water (a syrupy mixture) was swallowed followed by measure- ment of blood glucose levels at 30 min intervals. The flux of glucose oxidation was measured by the appear- ance of 3H2O in the blood stream. While the information The diagram to the right compares the rate 8000 ORAL GLUCOSE 6000- 4000- 2000- -120 -60 60 120 180 240 300 Minutes cannot be directly extracted from the reaction mecha- nism diagrams in the textbook, the glycolytic step in which the tritium is first released into water is that catalyzed by TPI, as illustrated at the beginning of Question #3. Explain why this step is suitable for measuring the flux of glycolysis through the release of °H…2. A 4-year-old girl was diagnosed with thiamine deficiency and the symptoms include tachycardia, vomiting, convulsions. Laboratory examinations reveal high levels of pyruvate, lactate and a-ketoglutarate. Explain which coenzyme is formed from vitamin B, and its role in oxidative decarboxylation of pyruvate. For that: a) describe the structure of pyruvate dehydrogenase complex (PDH) and the cofactors that it requires; b) discuss the symptoms which are connected with the thiamine deficiency and its effects on PDH and a-ketoglutarate dehydrogenase complex; c) explain the changes in the levels of mentioned metabolites in the blood; d) name the deseribed discase,1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: དང་ NH₂ ODH ས HO S མིནྟཱ ཨཱར པ 'ནཔི ཏཏྭཱ ཡཾ དསྨཱ ཨབྷིནྡནྟི ཨཱ R₂ OH NAD(P)H NAD(P)* R OH R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). : The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…
- In the skeletal muscle, in anaerobic conditions, glyceraldehyde 3-phosphate is converted into pyruvate during the payoff phase of glycolysis; and this pyruvate is reduced into lactate during lactic fermentation. Part 1-Write the 11 balanced biochemical equations corresponding to all the reaction steps leading to the conversion of glyceraldehyde-3-phosphate into lactate through glycolysis followed by lactic fermentation. Part 2-Write the net equation of the whole transformation process (i.e. with glyceraldehyde-3-phosphate as the starting substrate; and lactate as the end product).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 B4) Phosphofructokinase (PFK) is a highly regulated enzyme in glycolysis. ADP (and also AMP - adenosine monophosphate) bind to allosteric sites on PFK's structure, causing additional active sites (fructose-6-phosphate binding sites) to open. Conversely, ATP and PEP (phosphoenolpyruvate) bind to different allosteric sites, resulting in PFK's active sites closing. a) How does an allosteric activator work? What is the allosteric activator? When would it be important for PFK to be activated? Function: Allosteric Activator(s): Importance: b) How does an allosteric inhibitor work? What is the allosteric inhibitor? When would it be important for PFK to be inhibited? Function: Allosteric Inhibitor(s): Importance: c) How does this relate to the ideas of homeostasis and why does it make sense to control this system homeostatically? Use a specific example to make your comparison.
- 1. Opine dehydrogenases (ODH) have evolved in invertebrate marine organisms with wide-ranging physiological roles. The first class of this family of enzymes provides an alternative pathway for the lactate dehydrogenase pathway in anaerobic energy production. The lactate dehydrogenase pathway is found in higher organisms and in mammals including humans. One class of opine dehydrogenases catalyzes the reductive coupling of pyruvate to N-a-carboxyalkyl-L-amino acids represented by the re- action below: NH₂ ི་ ODH HO R 요 OH སྨིཾནྟཱ ར པ དརཱ ཨཱཋཏྭཱ… … ཨཱསྨིཾ ཏྟཏྟིནྡནྟི ཨཱ HO NAD(P)H NAD(P)* S R₁ R₂ where R1 is the side chain of the amino acid, R2 represents the alkyl group of the a-keto acid that is coupled to the amino acid, and NAD(P)H/NAD(P)* are the reduced/oxidized forms of nicotinamide ad- enine dinucleotide phosphate, a cofactor of the enzyme that catalyzes oxidation-reduction reactions. (a). The product of the reaction has two chiral centers as shown: The Ca atom of the amino acid…3. Pyrozole has been proposed as a possible nontoxic inhibitor of LADH-catalyzed ethanol oxidation. Its kinetics have been studied and, in 2 separate experiments, the velocity of the reaction was measured as a function of [C₂H5OH] and of [NAD+]. The data is given in the tables below. [C₂H5OH] varies, [LADH]= 4µg/ml, [NAD+] = 350 µM, pH=7.4, 23.5C [C₂H5OH] Vo (relative units) Vo (relative units) 1x10-5 M pyrazole M No pyrazole 2.1 1.8 1.5 1.35 0.008 0.002 0.001 0.00067 Vo (relative units) No pyrazole 0.00011 1.7 0.000056 1.4 0.000033 1.3 0..000017 0.95 1.7 1.0 [NAD+] varies, [LADH]= 4µg/ml, [C₂H5OH]= 5 mM, pH=7.4, 23.5C [NAD+] Vo (relative units) 4x10-5 M pyrazole 0.69 0.52 0.85 0.71 0.63 0.47 a. Plot the data as Lineweaver-Burke plots on two separate graphs. b. Determine the Km values for [C₂H5OH] and of [NAD*]. (You can't find Vmax because the exact units of Vo are not provided) c. What type of inhibition is exhibited by pyrazole against C₂H5OH is a substrate? Describe what is going…
