is an enzyme that exhibits covalent catalysis is the name of the metal present in the active site of carbonic anhydrase is the name of the reagent used to poison serine proteases
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- 8. In patients with diabetes mellitus type 1, the biochemical disorders result from changes in fuel metabolism. One of these signs is acidosis, Explain why such patients have a deviation of blood pH from the norm? For this 9. b) write the reactions of synthesis and oxidation of these molecules, name the enzymes, coenzymes, reaction localization: XConsider this mechanism of enzyme action: Urease can catalyze the hydrolysis of Urea, H,N – C – NH, II but not H H the hydrolysis of diethyl urea N -C - C;H5 C2H5 Explain this action.A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
- Which of the following enzymes requires a cofactor to carry out catalysis? A- GI lipase B- HIV protease C- Aldehyde dehydrogenase D- Epoxide hydrolase E- Beta-Lactamasei) Re-arrange the Michaelis Menten equation so it involves the ratio [S]. Show all steps beginning Km noting any assumptions or required conditions. Km ii) Calculate the ratio [lo for the case when the rate of product formation is 68% of Vmax and the substrate is in great excess. d[P] dt : k₂ with = [E],[S] Km+[S]' [S]o Km iii) Explain, in a few sentences, why the ratio determines the ratio V Vmax V Vmax Begin by explaining the meaning of stating simply "it's the ratio...." is not sufficient. Include in your explanation the factors that effect v and Vmax. Consider what factors make v different from or equal to Vmax. Consider what Km represents concerning processes involving ES. " iv) Calculate KM at 310K at given the following rate constant information: k₁ = 17 s-¹M-1 at 300K with A = 7300 s-¹M-1 K-1₁ 6 s¹ at 300K with A = 14500 s -1 k₂ = 31 s¹ at 300K with A = 600 s-¹Give a complete and well descriptive definition of the following:1.1 Fractional saturation1.2Allostery1.3 Metal activated enzymes 1.4 Metalloenzymes1.5 Acid-base catalysis
- Given the active site diagram below, identify the mechanism(s) of catalysis. 5 2 Metal ion Induced Fit Acid-base HN S is. By Approximation Acid-base, Metal ion -3 4There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.Diazepam is converted in vivo to an active metabolite Oxazepam. Explain metabolic transfomation of diazepam to oxazepam. (Provide names of enzymes involved in this transformation. Drawings of structures ofintemediate metabolites is NOT required)
- Bypass reaction in the anabolic pathway often occurs when A The ΔG of the reverse reaction in the catabolic pathway has a large negative value B The ΔG of the reverse reaction in the catabolic pathway has a large positive value C The ΔG of the reaction in the anabolic pathway is close to zero D The ΔG of the reaction in the anabolic pathway is positive E None of the aboveAerobic degradation of an organic compound by mixed cultureof organism in wastewater can be represented by following reaction. C3H6O3 + a O2 + b NH3 → c C5H7NO2 + d H2o + e CO2 A. Determine a, b, c, d and e, if YX/S = 0.4 d X/g S. B. Determine the yield coefficients YX/O2 and YX/NH3. C. Determine the degree of reductions for the substrate, bacteria and RQ for the organisms3. b. If chymotrypsin is treated with disopropylfluorophosphate, catalysis cannot occur even in the presence of excess substrate concentration. Is this Inhibltion reversible or Irreversible?. Dilsopropylfluorophosphate Hyd