Draw curved arrows to show the mechanism for the step of the B-ketoacyl-ACP synthase reaction shown below. Arrow-pushing Instructions :0: :0: :0: :0: ACP LACP H2C H2 :ö:
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- Lysine catabolism begins with reductive amination of a-ketoglutarate to give saccharopine in a multistep process. Draw curved arrows to show the movement of electrons in this step of the reaction mechanism. Arrow-pushing Instructions 7 COO H NH3 COO OOC B: COO H NH3 COO BH+Draw curved arrows to show the mechanism for the step of the HMG-synthase reaction shown below. Arrow-pushing Instructions H. :0: :OH :ÖH :0: CoA COA COA но ČH3 :OH ČH3 CoA1 Norepinephrine can be metabolized to the following metabolite in two steps as shown below. What might be the enzymes (in the correct order) responsible for these biotransformations? но но но HN -OH но- но но Он OH OH norepinephrine COMT / MAO MAO / Cyp450 MAO / Aldehyde dehydrogenase Сур450 / МАО
- Draw curved arrows to show the mechanism for the step of the B-ketoacyl-ACP synthase reaction shown below. Arrow-pushing Instructions :0: :0: :0: :0: LACP ACP H2C H2 :ö:The following figure shows the intermediate of the transketolase mechanism. Use arrow pushing to form the resonance stabilized enzyme intermediate. Show the mechanism for reaction of this intermediate with the given aldose, using the protonated acid/base residue suppliec by the enzyme. Clearly show the product of the reaction and make sure that the acid/base residue ends up in the protonated state at the end or your mechanism. H. CH,OH H-B H- HO- OH H- OH CH,OPO,Draw the electron pushing reaction mechanism for the hydrolysis of the artificial sweetener aspartame, a potential substrate of chymotrypsin, under acid, base and enzymatic conditions.
- One of the steps in the pentose phosphate pathway for glucose catabolism is the reaction of xylulose 5-phosphate with ribose 5-phosphate in the presence of a transketolase to give glyceraldehyde 3-phosphate and sedoheptulose 7-phosphate. (a) The first part of the reaction is nucleophilic addition of thiamin diphosphate (TPP) ylide to xylulose 5-phosphate, followed by a retro-aldol cleavage to give glyceraldehyde 3-phosphate and a TPPcontaining enamine. Show the structure of the enamine and the mechanism by which it is formed. (b) The second part of the reaction is addition of the enamine to ribose 5-phosphate followed by loss of TPP ylide to give sedoheptulose 7-phosphate. Show the mechanism.One of the steps in the pentose phosphate pathway for glucose catabolism is the reaction of sedoheptulose 7-phosphate with glyceraldehydes 3-phosphate in the presence of a transaldolase to yield erythrose 4-phosphate and fructose 6-phosphate. (a) The first part of the reaction is the formation of a protonated Schiff base of sedoheptulose 7-phosphate with a lysine residue in the enzyme followed by a retro-aldol cleavage to give an enamine plus erythrose 4-phosphate. Show the structure of the enamine and the mechanism by which it is formed. (b) The second part of the reaction is a nucleophilic addition of the enamine to glyceraldehyde 3-phosphate followed by hydrolysis of the Schiff base to give fructose 6-phosphate. Show the mechanism.Please draw by hand. Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme's catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a base and an acid catalyst, respectively. Propose a mechanism for the reaction. ОН 2-03Р0 ОН dihydroxyacetone phosphate triosephosphate isomerase 2-03РО. H glyceraldehyde-3-phosphate FYI Glu is glutamic acid and his is histadine
- Imidazoleglycerol‑phosphate dehydratase is an enzyme in the histine biosynthesis pathway. It catalyzes the E1 dehydration of D‑erthyro‑imidazole‑glycerol phosphate to imidazole acetol‑phosphate. This is a rare example of a biological E1 reaction, as most biological elimination reactions occur through E1cB instead. In this reaction, D‑erthyro‑imidazole‑glycerol phosphate is first protonated to form a good leaving group. Then, the leaving group is ejected to form the resonance‑stabilized carbocation shown. Draw curved arrows forming the most stable resonance structure to explain why this reaction goes through an E1 mechanism. Draw curved arrows to form the most stable resonance structure.The rate constant for the uncatalyzed reaction of two molecules of glycine ethyl ester to form glycylglycine ethyl ester is 0.6 M- 1s - 1. In the presence of Co2 +, the rate constant is 1.5 * 106 M- 1s - 1. What rate enhancement does the catalyst provide?If a chemist attempted to carry out the coupling of the two a-ketoacids shown in the mechanism WITHOUT using the enzyme, what product (or products) would you expect? (I'm providing the whole mechanism here again to help you consider this question.) OH CH;- CH OH 00 CH CH;CH, R 10 B: H, ОН CH, CH, ČH,CH, R- HO `CH,CH3 CH CH,CH, CH CH;CH, HO HO `CH,CH3 НО `CH3 HO `CH3 CH,CH; A C D O only D all of these would be possible O only A O only B only C