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- . Using the principles described in the text regarding pyridoxal phos- phate mechanisms, propose a mechanism for the reaction catalyzed by serine hydroxymethyltransferase.. Consider the enzymatic reaction scheme: Asparagine + H20 Aspartate + NH3: a) calculate the specific activity of the enzyme, if in 30 seconds as a result of a reaction involving 3 mg of the enzyme under optimal conditions (pH 8.0, 37 °C) 75 umol aspartate is obtained; b) describe the reasons for the decrease in enzyme activity after incubation for 6. 10 minutes at 70 °C (provide an appropriate graph).Describe the mechanism of a-chymotrypsin. Explain the roles of constituents of the catalytic triad, their modes of catalysis, and the significance of the oxyanion hole in the catalysis.
- . The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.Explain the biochemical importance of the components of the cholesterol biosynthetic pathway.Consider the complete oxidation of a mixed TAG containing the following fatty acid residues:At carbon 1: cerotic acidAt carbon 2: heptadecanoic acidAt carbon 3: palmitoleic acid Draw the structure of the mixed TAG.
- Describe the application of transamination in the biosynthesis of shikimate derivatives. Show how the isoflavone is obtained from flavanones. What is the primary reaction involved?Consider applying biocatalytic reduction with carrots to the following two ketones: tert-butyl methyl ketone, and 3-hexanone. Which would you expect to give higher enantioselectivity in biocatalytic reduction? Explain your answer.(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?
- Write the mechanism (in detail) for the conversion of aspartate and carbamoyl phosphate into N - carbamoylaspartate. Include a role for the histidine residue present in the active site.Using the principles described in the text regarding pyridoxal phosphate mechanisms, propose a mechanism for the reaction catalyzed by serine hydroxymethyltransferase.(b) The values of kinetic parameters for a variety of synthetic ester and peptide substrates ofa- chymotrypsin are compared for the reaction scheme below where ES is the Michaelis complex, ES' E+S Substrate K₁ N-Ac-Trp–OC₂H5 N-Ac-Phe-OC2H5 N-Ac-Leu-OC2H5 N-Ac-Phe-CONH2 N-Ac-Tyr-p-nitro-anilide ES K₂ 3.5 13.0 3.2 1.7 K-₁ is the acylenzyme, P₁ is the first product to be released, P2 is the second product, k2 is the acylation rate constant, k3 is the deacylation rate constant, and kcat = k2 k3/( k2 + k³). In the table below, N- Ac = N-acetyl; -CONH₂ = carboxamide; -OC₂H5 = ethyl ester; p-nitroanilide = −NH-C6H4-NO2 simulating a peptide group. ES' K2 (S-¹) K3 (S-1) 0.84 2.2 0.19 P₁ K3 0.073 H → E+ P2 Kcat (S-1) 0.82 1.9 0.18 0.070 0.038 KM (MM) 0.08 1.3 4.2 24.0 0.35 1 Kcat/ KM (mM-¹ s¯¹) 10.3 1.5 0.04 0.003 0.11 The value of kcat for N-Ac-Phe-OC2H5 is two-fold greater than that for the L-tryptophanyl analog and more than 10-fold greater than the value of kcat for the ester substrate…
