2. Cells often use the same enzyme reaction pattern for analogous metabolic conversions. For example, the steps in the oxidation of pyruvate to acetyl-CoA and of a-ketoglutarate to succinyl-CoA, although catalyzed by different enzymes, are very similar. The first stage of fatty acid oxidation follows a reaction sequence closely resembling a sequence in the citric acid cycle. Use equations to show the analogous reaction sequences in the two pathways.

2. Cells often use the same enzyme reaction pattern for analogous metabolic conversions. For example, the steps in the oxidation of pyruvate to acetyl-CoA and of a-ketoglutarate to succinyl-CoA, although catalyzed by different enzymes, are very similar. The first stage of fatty acid oxidation follows a reaction sequence closely resembling a sequence in the citric acid cycle. Use equations to show the analogous reaction sequences in the two pathways.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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1. Consider the oxidation of the fatty acid with the common name arachidic acid. a. Draw the structure of arachidic acid. b. How many turns of the fatty acid oxidation cycle is required for the complete oxidation of arachidic acid? c. How many moles of ATP are formed from one mole of arachidic acid if the acetyl CoA produced go to the citric acid cycle and oxidative phosphorylation? Assume 1 mole of NADH is equivalent to 3 moles ATP and 1 mole FADH2 is equivalent to 2 moles of ATP. Show how you arrived at your answer
1 The carbon skeletons of amino acids can be catabolised via various steps. These end products are often intermediates of the citric acid cycle. 100X0 0801 For example: Valine →→→succinyl-CoA Arginine →→→ a-ketoglutarate Aspartate →→→→ oxaloacetate What is the theoretical ATP yield from the catabolism of the end product of valine degradation feeding into the citric acid cycle? OND OND (Your answer should consider ATP production from the citric acid cycle up until oxaloacetate, as well as electron transport chain-mediated production of ATP. Your answer should be a number, without any other text. E.g.: 2. The image below has been provided to help you.):00:0 Acetyl-CoA NADH Oxaloacetate Malate Fumarate 1. 040 Citrate Isocitrate * a-ketoglutarate f Succinyl-CoA CO2 CO₂ NADH NET 16. 0 10:00:0ONDI NADH DOROHOI
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
6. The AG of the citric acid cycle reaction catalyzed by succinyl-CoA synthetase is approximately 0 kJ/mol. Which of the following statements explains why we would expect this reaction to be highly exergonic, but why the overall AG = 0 in reality. A) The reaction cleaves a thioether linkage, and the released free energy is used to generate a new thioester linkage in a product molecule. B) The reaction cleaves a thioester linkage, and the released free energy is used to generate GTP. C) The reaction cleaves a thioester linkage, and the released free energy is used to generate a new thioester linkage in a product molecule. D) None of the above
1. Explain the reaction mechanism involved how glucogenic amino acids can yield either a pyruvic acid or an oxaloacetic acid. In what pathway will pyruvic or oxaloacetic acid be used and why is this pathway important? 2. Discuss the reaction mechanism involved how the -NH2 groups of amino acids are being metabolized. 3. Explain why gluconeogenesis under conditions of starvation or diabetes breaks down body proteins. Complete answer please. Thank you. |
2. The enzyme exists in two interconvertible forms that differ markedly in their activities: Protomer (inactive) ⇒ filamentous polymer (active) Citrate and isocitrate bind preferentially to the filamentous form, and palmitoyl-CoA binds preferentially to the protomer. Select the true statements that explain how these properties are consistent with the regulatory role of acetyl-CoA carboxylase in the biosynthesis of fatty acids. High citrate and isocitrate levels indicate that there is plenty of ATP, reduced pyridine nucleotides, and acetyl-CoA for fatty acid synthesis. Palmitoyl-CoA is a feedback inhibitor, driving the equilibrium in the direction of the inactive (protomer) form. Palmitoyl-CoA triggers phosphorylation to inactivate the enzyme. Citrate and isocitrate are the precursors for acetyl-CoA synthesis in the mitochondria, thus providing the starting material for fatty acid biosynthesis. The protomer and filamentous polymer are the two subunits of acetyl-CoA carboxylase that hold…
8. The enzyme thiolase catalyzes one step in the ß-oxidation of saturated fats. One portion of the mechanism for this reaction is shown below. Describe the catalytic mechanism at work. (Note: "SCOA" is shorthand for the compound Acetyl-CoA) RCOCH₂COSCoA + HSCOA → H3C₂OSC0A + RCOSCOA HN NH CH₂ NH CH₂ CH₂ FS Grease NH3 H-SCO A NH CH2 CH₂ NH3 S Co A CH₂ NH 1 3 H-SCO A H3C SCO A NH3 a h-SCOA R-C S Co A CH₂ CH₂ C H₂ 0=0 HN NH + NH3 H₂C HN CH₂ NH CH₂ CH₂ 2 S Co A CH₂ NH NH
1. The enzyme glutamate dehydrogenase is important in the breakdown of amino acids to produce NH4+. High levels of NH4+ in the body are toxic, and for this reason it is used to form urea to be excreted in the urine. Using the information provided, calculate the delta G knot prime and the Keq value at 298K for the oxidation of glutamate catalyzed by glutamate dehydrogenase. (Constants: R=8.3J/degree.mol, F=96.1kJ/V.mol) How to identify the final and initial reactions in a group of redox reactions and do we reverse the reduction reaction if the question asks for oxidation?
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1.The diagram below shows an outline of the aminotransferase mechanism that skips the specific steps that show how electrons flow when a Schiff base is formed or is hydrolyzed. Using the mechanistic details given below A. Draw the mechanism for Enzyme- PLP Schiff base formation using pyridoxal and the lysine amine group using arrow to indicate electron flow. B. Draw the mechanism for hydrolysis of the Schiff base to form the a-keto acid, which is the reverse of the first reaction. Stage 1 Lys residue 2-O,PO- Enz Amino acid Lys residue (CH2)4 (CH₂2)4 H R-C-COO R- NH₂ NH₂ R-C-COO *NH₂ H H- 2-0,PO- 2-0,PO- A. show how this forms Stage 1 Lys residue Enz (CH2)4 HO 2-O,PO Enzyme-PLP Schiff base OH Amino acid-PLP Schiff base (aldimine) LOH 2-0₂PO- OH 20,PO- a-Keto acid COO Ketimine a-Keto acid 2-0,PO- R-C- NH₂ B. show how the a-keto acid forms a-Keto acid H Enzyme-PLP Schiff base الرواية وطري Ketimine Pyridoxine (vitamin B6) Pyridoxal phosphate (PLP) Pyridoxamine phosphate Stage 2 Amino acid…
8. Compare the energy cost, in ATP equivalents, of synthesizing stearate from mitochondrial acetyl-CoA to the energy recovered by degrading stearate to acetyl-CoA. assume NADH (or NADPH) and FADH2 yield 2.5 and 1.5 ATP equivalents, respectively. Remember that FAS stops at palmitate; the pathway for further elongation is shown in the book (Fig. 20-28). Don’t forget steps needed to generate malonyl-CoA or transport of acetyl-CoA out of the mitochondria. Please show me detailed solution.
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