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- Draw 10 H-bonds between the below compound (coenzyme A) and water moleculesBased on this graph, it appears that carboxylesterase is most active at a pH of A. 3.5B. 1.5C. 5D. 4In the conversion of acetone to aceto-cyanohydrin, the effect of electron-donating substituents on the tetrahedral intermediate is to: destabilize the charge on oxygen destabilize the carbocation formed make the intermediate more crowded stabilize the charge on oxygen
- The oxidation of 1 mol of glucose supplies enough metabolic energy to form 36 mol of ATP. Oxidation of 1 mol of a typical dietary fat like tristearin (C57H116O6) yields enough energy toform 458 mol of ATP. How many molecules of ATP can form per gram of (a) glucose; (b) tristearin?1. Provide the best coenzyme(s) for each step shown below. Give a 1–2 sentence rationale for your choice. 2. Reaction (C) can require multiple coenzymes, or the enzyme may only require one. Briefly describe how the reaction that uses only one coenzyme works. Be specific about the mechanism.Enzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. a Tyr residue on the enzyme is involved in the reaction. a His residue on the enzyme is involved in the reaction the enzyme uses NADH has a cofactor. the enzyme uses coenzyme A has a cofactor.
- Provide the structure of the REACTANTS and PRODUCTS Step Reactants/ substrates Enzyme function Product 1 Acetyl CoA and acyl-carrier protein(ACP) and Malonyl CoA and ACP Acetyl transacylase and Malonyl transacylase transfers the acyl and the malonyl moiety to the holo-ACP molecule. Acetyl ACP and CoA and Malonyl ACP and CoA 2 Acetyl ACP and Malonyl ACP acyl-malonyl ACP condensing enzyme catalyzes the condensation reaction. Acetoacetyl ACP 3 Acetoacetyl ACP beta-ketoacyl ACP reductase enzyme catalyzes the reduction reaction and the NADPH is used as the reducing agent. D-3-hydroxybutyryl ACP. 4 D-3-hydroxybutyryl ACP. 9-hydroxyacyl ACP dehydratase enzyme catalyzes the dehydration reaction. Crotonyl ACP 5 Crotonyl ACP Enoyl ACP reductase enzyme catalyzes the reduction reaction. Butyryl ACP 6 Butyryl ACP condensation reaction C6-beta-ketoacyl ACP 7 C6-beta-ketoacyl ACP Ketoacyl-ACP reductase catalyzed the reduction reaction C6-acyl ACP 8 Palmitoyl ACP…Provide the structure of the REACTANTS and PRODUCTS Step Reactants/ substrates Enzyme function Product 1 Acetyl CoA and acyl-carrier protein(ACP) and Malonyl CoA and ACP Acetyl transacylase and Malonyl transacylase transfers the acyl and the malonyl moiety to the holo-ACP molecule. Acetyl ACP and CoA and Malonyl ACP and CoA 2 Acetyl ACP and Malonyl ACP acyl-malonyl ACP condensing enzyme catalyzes the condensation reaction. Acetoacetyl ACP 3 Acetoacetyl ACP beta-ketoacyl ACP reductase enzyme catalyzes the reduction reaction and the NADPH is used as the reducing agent. D-3-hydroxybutyryl ACP. 4 D-3-hydroxybutyryl ACP. 9-hydroxyacyl ACP dehydratase enzyme catalyzes the dehydration reaction. Crotonyl ACP 5 Crotonyl ACP Enoyl ACP reductase enzyme catalyzes the reduction reaction. Butyryl ACP 6 Butyryl ACP condensation reaction C6-beta-ketoacyl ACP 7 C6-beta-ketoacyl ACP Ketoacyl-ACP reductase catalyzed the reduction reaction C6-acyl ACP 8 Palmitoyl ACP…Draw a 6-carbon saturated fatty acid and show where the double bond is created during the first step of β-oxidation. What is the orientation of this bond?
- DRAW IT Start with the linear form of fructose (see Figure 5.3) and draw the formation of the fructosering in two steps, as shown in (a). First, number the carbons starting at the top of the linear structure.Then draw the molecule in a ringlike orientation, attaching carbon 5 via its oxygen to carbon 2. Comparethe number of carbons in the fructose and glucose rings.TRUE OR FALSE 1. Abzymes reduce rotational entropy. 2. Hammerhead ribozymes have the ability to bind more efficiently and recognize. 3. Metal ion catalysts act as electrophilic catalysts, stabilizing electron density that can develop during reactions.The structure of a metalloenzyme active site is down below(black picture). Describe, from a chemical and structural perspective, how the reactive site is designed to facilitate its catalytic reaction. The example below(white pitcure) suggests the level of detail that is required. Make sure that you explain what the metal is doing, what the reaction is, and its biological significance.