23.Show by the movement of electrons (via the use of arrows) how oxaloacetate isdecarboxylated in the presence of GTP to form phosphoenolpyruvate. Correctly place the startingpoint and ending point of your arrows.O=CCH2LOGuanosine-PIOIOO-POH2C CCOO용용이CO2 + GDPO

The image depicts the conversion of oxaloacetate to phosphoenolpyruvate (PEP) in the presence of…

Answered: 23. Show by the movement of electrons…

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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4) Suppose some yeast cells undergoing gluconeogenesis were treated with a 1:1 mixture of the two labeled pyruvate molecules shown below (one pyruvate is labeled with ¹4C at C1 and ¹³C at C3; the other pyruvate is labeled with ¹4C at C3 and ¹3C at C2. Assume that the labeled pyruvate molecules are the only source of carbon to make glucose via gluconeogenesis. Draw the resulting mixture of glucose molecules and clearly show the location of ¹4C and/or ¹³℃ in each glucose. 13CH3 14CH3 13C
The phosphorylation and oxidative decarboxylation of oxaloacetate by inorganic phosphate (Pi) to make phosphoenolpyruvate and carbon dioxide is endergonic under intracellular conditions. It is characterized by this equation: Oxaloacetate + Pi ←→ Phosphoenolpyruvate + H2O + CO2 ΔG’ = +24.6 kJ/mol The synthesis of GTP from GDP and inorganic phosphate (Pi) in solution is endergonic under intracellular conditions, and it is characterized by this equation: GDP + Pi ←→ GTP + H2O ΔG’ = +30.5 kJ/mol Write a new net thermodynamically coupled reaction equation that describes the synthesis of phosphoenolpyruvate from oxaloacetate using the hydrolysis of GTP to power the reaction and calculate the new net ΔG’ of this reaction. Show all of your work.
Prostaglandins are a group of lipid compounds having diverse hormone-like activities in animals. They are biosynthesized from the fatty acid arachidonic acid, catalyzed by the enzyme cyclooxygenase. The biosynthesis involves via a multistep radical mechanism. Can u show me in a stepwise mechanism how it is converted from radical intermediate A to prostaglandin PGG2.
Identify each reaction catalyzed by (a) a nucdeotidase; (b) a phosphorylase; (c) a phosphoribosyltransferase. GMP A D E Guanine Guanosine F
The glutamate dehydrogenase (GDH) catalyses the following reaction: +H₂N- H - - CH₂ - CH₂ COO acide glutamique COO™® + NAD+ + H₂O GDH COO C: CH₂ CH₂ COO™ O + NH4+ NADH + H* The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: -0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min - Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. acide a-cétoglutarique The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data: ENADH at 340 nm = 6220 M¹.cm¹ Time (min) 1 2 3 4 5 6 7 8 9 1.760 1.718 1.675 1.635 1.595 1.550 1.510 1.489 1.476 A340 10 1.451 - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. - Comment the shape of the curve, particularly the portion that corresponds to a…
16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³(aq) + 2HPO(aq) + 2H₂O(1) 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP4 (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
10 ATP/Acetyl-CoA * 2 acetyl-CoA = 20 ATP 1 GTP/ Acetyl-CoA * 2 acetyl-CoA = 2 GTP 1,5 ATP/ FADH2 * 1 FADH2= 1,5 ATP 2,5 ATP/ NADH * 3 NADH = 7,5 ATP 7,5 + 1,5 + 20 = 29 ATP och 2 GTP All of this is round off, how to calculate without rounding off? 2-Acetyl-CoA and 15 subunits
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4) 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.

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23. Show by the movement of electrons (via the use of arrows) how oxaloacetate is decarboxylated in the presence of GTP to form phosphoenolpyruvate. Correctly place the starting point and ending point of your arrows. O=C CH2 LO Guanosine- PIO I O O-PO H2C C COO 용용이 CO2 + GDP O