Devise a biosynthesis for the natural product (II) from an appropriate starter co-enzyme A and malonyl coenzyme A. appropriate starter molecule (I) S-COA malonyl coenzyme A By (II)
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- please explain why this happends, im having trouble in this section. Part A Chymotrypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?Sterol Biosynthesis A) Name the enzymes and draw the reactions for the synthesis of lanosterol from hydroxymethylglutaryl-Co B) Identify and draw the mechanism of the steps of the prenyltransferase reaction. C) Define statin and identify which enzyme is inhibited by statins.A is a key intermediate in an enzyme mediated reaction. A immediately reacts further to give B and C. Provide mechanisms to explain the formation of B and C. The reaction takes place in H2O (solvent).
- The following compound has been found to be an inhibitor of penicillinase. The enzyme can be reactivated by hydroxylamine (NH2OH). Propose a mechanism to account for the inhibition and for the reactivation.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.Ozonolysis, osmylation, and epoxide formation with mCPBA are all what type of reactions? a.) reduction b.)oxidation c) bothd) neither
- tert-Butoxycarbonyl azide was developed as a reagent for peptide synthesis at OWL's home institution, the University of Massachusetts, by Prof. L.A. Carpino. It is prepared by treating tert-butoxycarbonyl chloride with sodium azide. Propose a structure for the initially-formed intermediate in this reaction.One of the later steps in glucose biosynthesis is the isomerization of fructose 6-phosphate to glucose 6-phosphate. Propose a mechanism, using acid or base catalysis as needed.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?
- The carbonyl group on D-glucose can be reduced to d-glucitol. Identify the reagents that can chrry out this reduction. A.water in acidic solution B. hydrogen with a Platinum catalyst (Hy/Pt) C. Sodium dichromate (NaCr2O) in acidic solution D. Benedict’s reagent E. EnzymesCarbonic anhydrase catalyzes the hydration of carbon dioxide: H2O + CO2 -> HCO3- + H+The following data is available: (image) - Calculate the Michaelis Menten constants - In the presence of sulfanilamide the Michaelis Menten constants for the reaction are Vmax: 7.57e-5M/s and Km: 20M. What type of compound is sulfanilamide and what is its mechanism of action?1. What reaction is catalyzed by the enzyme carbonic anhydrase? Which metal ion serves as a cofactor for carbonic anhydrase? Explain how this metal ion is able to assist in catalyzing the reaction. 2. In relation to enzymes, what is the difference between a cosubstrate and a prosthetic group? Give one example of each.