[AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions.
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![[AktivGrid] Draw the product
of the reaction of isocitrate
catalyzed by isocitrate
dehydrogenase in the TCA
(citric acid) cycle. Provide
the structure in the
protonation state found in
physiological conditions.
rxn'
F-C-H
NAD+
isocitra
te
dehydro
genase
NADH,
Dra
H+,
>
Problem 5 of 12
Submit
H
Atoms, Bonds
and Rings
OH
Charges
CH2OH
Drag To Pan
CH2OH-
H
OH
Undo
Reset
―CH2OH-
Remove
Done
⚫SH
CHO
+](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F4bf2ee70-3310-46f0-8447-d007eb9e1b43%2F3726d1f3-d1de-422d-9371-c34d076b0bfe%2Fb8ppsfg_processed.png&w=3840&q=75)
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- Because of the position of arsenic in the periodic table, arsenate (AsO43- ) is chemically similar to inorganic phosphate and is used by phosphaterequiring enzymes as an alternative substrate. Organic arsenates are quite unstable, however, and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.[AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions. 9 H-C-OH 800- -H CH₂ ° Coo of NAD+ dehydrogen isocitrate ase NADH, H*, Drawing CO2, which indicates AG for each glycolytic reac- tion under intracellular conditions. Assume that glyceraldehyde-3- phosphate dehydrogenase was inhibited with iodoacetic acid. Which glycolytic intermediate would you expect to accumulate most rapidly, and why?
- #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)If a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.(b) the activity of the malate-aspartate shuttle (MAS) system of isolated rat brain mitochondria suspended in an isotonic me- dium buffered to pH 7.4. Diagram A illustrates NADH fluo- rescence emission upon addition of Glutamate in the ab- sence and presence of Aspartate. Diagram B illustrates sim- ilarly NADH fluorescence emission upon addition of Gluta- mate in the presence of Aspartate followed by additions of submicromolar concentrations of Ca2+. As is well estab- lished, the MAS in brain, skeletal muscle, and cardiac mus- Diagrams A and B on the right show changes in Glu A Glu В -No Asp + 0 +0.12 -0.48 + 16 0.81 +1.8 ++ Asp 10 min 2 min cle mitochondria is activated by cytosolic concentrations of Ca2* < 3 µM. To simulate the cytosolic part of the MAS, the following reagents were added to the medium: 4 units/ml glutamate-oxaloacetate transaminase, 6 units/ml malate dehydrogenase, 66 µM NADH, 5 mM aspartate, 5 mM malate, 0.5 mM ADP, 200 nM ruthenium red (to block the mitochondrial…
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH <=> Lactate + NADH+H+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b.The interconversion of DHAP and GAP greatly favors the formation of DHAP at equilibrium. Yet the conversion of DHAP by triose phosphate isomerase proceeds readily. WhyCertain microorganisms with a modified citric acid cycle decarboxylate a-ketoglutarate to produce succinate semialdehyde: (a) Succinate semialdehyde is then converted to succinate, which is furthermetabolized by standard citric acid cycle enzymes. What kind of reactionis required to convert succinate semialdehyde to succinate? Showany coenzymes that might be involved.(b) Based on your answer in part a, how does this pathway compare to thestandard citric acid cycle in energy yield?
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1In addition to consumption by glycolysis, glucose 6-phosphate is used to generate other 5. (a) key cellular metabolites – including precursors for nucleic acids and modulators of cellular red/ox bal- ance – via the oxidative phase of the pentose phosphate pathway. What nucleic acid precursor mole- cule and what key cofactor are generated by the oxidative phase of the pentose phosphate pathway? Draw the reactions including all reactants and products that comprise this phase of the pathway.