Hw.3. OHACPSuppose that a "snapshot" of FA synthase was taken and the above (drawn) intermediate (STRUCTURE X) is shown in the active site of FAS I.What chemical equations (below) best explains what would happen in the NEXT 2 reactions to create C8:0-ACP? Assume that FA synthesis occurs inthe proper sequential order.O Structure X + NADPH + H+ --> NADP+ + C6:0-ACP + H₂OO Structure X + NADPH + H+ --> NADP+ + C6:0-ACPO Structure X + 2 NADPH + 2 H+ --> 2 NADP+ + C6:0-ACPO Structure X + 2 NADPH + 2 H+ --> 2 NADP+ + C6:0-ACP + 1 CO2O Structure X + 2 NADPH + 2 H+ --> 2 NADP+ + C6:0-ACP + 1 CoA + H₂O

The given reaction is from fatty acid biosynthesis that occurs in the cytoplasm. Fatty acid…

Answered: OH i ACP Suppose that a "snapshot" of…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter21: Photosynthesis

Section: Chapter Questions

Problem 8P

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The Relative Efficiency of ATP Synthesis in Noncyclic versus Cyclic Photophosphorylation If noncyclic photosynthetic electron transport leads to the translocation of 7 H+/2e- and cyclic photosynthetic electron transport leads to the translocation of 2 H+/e-, what is the relative photosynthetic efficiency of ATP synthesis (expressed as the number of photons absorbed per ATP synthesized) for noncyclic versus cyclic photophosphorylation? (Assume that the CF1CF0-ATP synthase yields 3 ATP/14 H+.)
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?
Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.
Understanding Enzyme Mechanisms Related to Pyruvate Carboxylase Based on the mechanism for pyruvate carboxylase (Figure 22.3), write reasonable mechanisms for the reactions that follow:
a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
Draw the pathway for the conversion of Propionyl CoA to Succinyl CoA as it occurs in thematrix of the mitochondria. Show the structures and names of all reactants and products, as well asthe names of the enzymes. You do not need to draw the structures of ATP, NAD+, CoA, etc., but doshow them as reactants or products in the appropriate places. You do not need to show themechanisms of the enzymes. Draw the pathway for the conversion of Succinyl CoA into 4 CO2. Show the structures andnames of all reactants and products, as well as the names of the enzymes. You do not need to drawthe structures of ATP, NAD+, CoA, etc., but do show them as reactants or products in the appropriateplaces. You do not need to show the mechanisms of the enzymes. How many ATPs would be generated by the complete oxidation of Propionyl CoA into 3 CO2using any of the required enzymes of -oxidation, gluconeogenesis, glycolysis,the citric acid cycle andoxidative phosphorylation?
If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.
The inhibitor X prevents coenzyme Q (Q) from participating in electron transfer in the electrontransport chain.(a) Will the presence of X prevent electrons from N ADH from passing through the electron trans-port chain? Explain why or why not.(b) Compound Y is a non-physiological reducing agent capable of directly reducing cytochromec1 in Complex III. Would oxygen consumption resume upon the addition of compound Y tomitochondria inhibited by inhibitor X? Be sure to explain your answer.
In steroid synthesis, squalene is oxidizedto squalene epoxide. This reaction is somewhat unusual, in thatboth a reducing agent (NADPH) and an oxidizing agent (O2) arerequired. Why are both needed?
You have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!
To carefully prepared mitochondria were added succinate, oxidizedcytochrome c, ADP, orthophosphate, and sodium cyanide. Referring toFigure 14.16, answer the following.(a) List the sequence of electron carriers in this system.(b) Write a balanced equation for the overall reaction occurring in thissystem, showing oxidation of the initial electron donor, reduction of thefinal acceptor, and synthesis of ATP.(c) Calculate ΔG°' for the overall reaction. ΔG°' for ATP hydrolysis is-32.2 kJ/mol.(d) Why was cyanide added in this experiment?(e) What would the P/O ratio be if the same experiment were run with addition to the mitochondria of 2,4-dinitrophenol?
With appropriate chemical reactions and with all the catalysts involved explain the differences between the MVA and MEP pathway.

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