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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- Devise a biosynthesis for the natural product (II) from an appropriate starter co-enzyme A and malonyl coenzyme A. appropriate starter molecule (I) + OiiS.COM malonyl coenzyme A → 'N (II)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?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.
- Following are the steps in the industrial synthesis of glycerin. Provide structures for all intermediate compounds (AD) and describe the type of mechanism by which each is formed.The formation of Br2 from NBS first involves the reaction of NBS with HBr to form an iminol intermediate and molecular bromine. The intermediate then undergoes acid-catalyzed tautomerism to form succinimide, the byproduct of the reaction. Propose a curved-arrow mechanism for the conversion of NBS into succinimide that also accounts for the formation of Br2.With a AG of -17 kJ/mol, the reaction catalyzed by hexokinase is considered to be at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the above
- 3a. 3b. 3c 3d. 3e. CO₂ clavulanic acid CH₂-OH H Answer the following questions about clavulanic acid. Does clavulanic acid inhibit D-alanyl-D-alanine transpeptidase? Does clavulanic acid contain a ß-lactam? Does clavulanic acid contain a thiazolium ring? What is the result of the treatment of penicillinase with clavulanic acid? Does clavulanic acid form a covalent acyl-enzyme intermediate with penicillinase?Carbonic anhydrase facilitates the dissolution of carbon dioxide gas into water by catalyzing its hydration. Is the catalyzed reaction efficient? By what criterion do you state that?If a solution of compound X is ncubated with a catalytic anount of enzyme Y the sucrose is trarsformed to glucose aid Euctose in the reaction 1X 1 fedose3 ghacose A eqahum, The concenttons of the seation comgoests he and 2mM glucose. What is Keg? Oa, 6 Ob4 Oa 20 O'd. 5 A Moving to another question wili save this response.
- c) Study the following reaction scheme for the preparation of a natural glycoside (compound 7) and answer the questions that follow: OH OAc Но excess Ac20 AcO pyridine, 0°C HO- Но. AcO- -OAc `0Ac HO Compound 3 Compound 4 HBr OCH3 OAc OAc AcO' AcO AcO AcO- OAc OAc Compound 6 Compound 5 Br NaOH, H2O OCH3 Он HO НО Compound 7 ii. Identify the unknown reagent(s) in the reaction scheme which converts compound 5 to compound 6.Covalent enzyme catalysis involves the formation of a transient covalent bond between an enzyme and its substrate Below is the general structure of a commonly encountered so-called acyl-enzyme intermediate Ent- NH OH+Ent Select amino acid residues from the table beliow that have side chains with the enzyme reactive groups indicated in the above reaction (if more than one, start with lowest numbered first. Amino acid No 3-detter code What is the chemical name of the acyl-enzyme intermediate compound (acylimidazole, anhydride, ester, Schif base, thioester? 2) 3 HN HO HO HO HO (5) 6 HN HD HO HN HO HO 03 15 HN HN HO HO HO HO 08 09 20 HOThe following reaction is: Ph Ph-p-In(CI)(PPH3)2 B-elimination H reductive elimination insertion oxidative addition H Ph₂P- -İn(CI) (PPH3)2 my flore