Draw the product of the reaction of acetyl CoA with ACP-SH catalyzed by malonyl-CoA-acetyl-CoA-ACP transacylase (MAT). Provide the structure in the protonation state found in physiological conditions.
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- Understanding the Mechanism of the HMC-CoA Synthase Reaction Write a suitable mechanism for the HMG-CoA synthase reaction. What is the chemistry that drives this condensation reaction?Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.Compare and contrast Pyruvate Dehydrogenase with a-ketoglutarate dehydrogenaseOutline the mechanisms of both enzymes. Discuss the functions of the coenzymes. List the similarities and the differences between the 2 enzymes. Both are very large membrane bound complexes. What are the advantages of this strategy?How detailed is the enzyme structure known below(It's Pyruvate Dehydrogenase )? What insight(s) does this structural detail give you about the enzyme mechanism.
- Consider docosanoic acid C12H43CO2H a. Label the alpha and beta Carbons. Show the beta-oxidation in an EXPANDED structure. b. Draw each acyl CoA derived from this fatty acid. c. How many acetyl Co A molecules are formed by complete beta-oxidation? d. How many cycles of beta-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid? Show the complete computation. f. How many moles of ATP per gram of fatty acid is formed from the complete catabolism of the given fatty acid? g. What is the molar mass of the given fatty acid? Solution: Show here the complete computations, [from a to e]Arrange the steps of breakdown of oleic acid (pictured below) in the correct order. 1 2 3 4 5 activation by acyl-CoAsynthe ✓ [Choose ] one cycle ofß-oxidationbeginning at the enoyl-CoAhydratasestep three cycles ofẞ-oxidation five cycles ofß-oxidation activation by acyl-CoAsynthetase enoyl-CoAisomeraseactivity enoyl-CoAisomeraseactivity V one cycle ofß-oxidationbegini V five cycles ofß-oxidation OHA. The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the active site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formu- las for Coenzyme A, ATP, and NADH. What is the largest structural fragment of each inhibitor that is responsible for competitive inhibition? Draw the molecular fragment common to each inhibitor that competes with the binding of acetyl-CoA in the active site of citrate synthase. Bromoacetyl-CoA ATP NADH K₁ (μM) 25.7 6800 8300 B While the inhibitor constants listed in part (b) above were determined in vitro for purified citrate synthase, does their inhibitory action have any relevance to the flux of metabolites through the TCA cycle in vivo? If so, explain.
- Incubation of the norsolinic acid synthase holo-ACP with malonyl CoA gave malonyl-S-ACP (molecular weight 10112 Da). (ACP SH holo-ACP Malonyl-SNAC Calculate the molecular weight of holo-ACP. (ACP OH malonyl-S-ACP MW = 10112Discuss the regulation of fatty acid metabolism by the isozymic forms of acetyl CoA carboxylase. Explain the reciprocal control of fatty acid synthesis and degradation and the various means by which this control is achieved(i) Consider a preparation that contains all the enzymes and cofactors necessary for fatty acid biosynthesis from acetyl-CoA and malonyl-CoA. If [2-H] acetyl-CoA labeled with deuterium, the heavy isotope of hydrogen and excess of unlabeled malonyl-CoA are added as substrates, where will you find these labeled deuterium atoms in a molecule of palmitate synthesized? Explain. S-COA (ii) Describe the steps involved in the synthesis of palmitic acid starting from acetyl-CoA and malonyl-CoA.
- Draw the product of the dehydration reaction of the B- hydroxyacyl-SACP catalyzed by B-hydroxyacyl-ACP dehydratase (DH) in the third elongation step of fatty acid synthesis. Provide the structure in the protonation state found in physiological conditions. OH B-hydroxyacyl-ACP dehydratase (DH) O Drawing SACP QCompare and contrast Pyruvate Dehydrogenase with a-ketoglutarate dehydrogenaseOutline the mechanisms of both enzymes. Discuss the functions of the coenzymes. List the similarities and the differences between the 2 enzymes. Both are very large membrane bound complexes. What are the advantages of this strategy?Do a bit or research on the structure one of these enzymes. (include one recent reference) – How detailed is the enzyme structure known? What insight(s) does this structural detail give you about the enzyme mechanism.The formation of acetyl-CoA from acetate is an ATP-driven reaction: Acetate + ATP + CoA Acetyl CoA + AMP + PP₁ Calculate AG" for this reaction given that the AG' for the hydrolysis of acetyl CoA to acetate and CoA is −31.4 kJ mol-¹ (−7.5 kcal mol¯¹) and that the AG°' for hydrolysis of ATP to AMP and PP; is -45.6 kJ mol-¹ (−10.9 kcal mol−¹ ). AG° reaction = AGO! i The PP, formed in the preceding reaction is rapidly hydrolyzed in vivo because of the ubiquity of inorganic pyrophosphatase. The AG" for the hydrolysis of pyrophosphate (PP;) is −19.2 KJ mol-¹ (-4.665 kcal mol-¹). Calculate the AGº' for the overall reaction, including pyrophosphate hydrolysis. reaction with PP, hydrolysis = What effect does the presence of pyrophosphatase have on the formation of acetyl CoA? kJ mol-¹ It does not affect the overall reaction. It brings the overall reaction closer to equilibrium. It makes the overall reaction even more exergonic. It makes the overall reaction even more endergonic. kJ mol-¹ -1