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- Lysozyme residues Asp 101 and Arg 114 are required for effi cient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not signifi cantly alter the enzyme’s tertiary structure, but it signifi cantly reduces its catalytic activity. Explain.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)The uncatalyzed reaction rate for the conversion of substrate X to product Y is one year. The enzyme-catalyzedrate is one millisecond. Describe the features of theenzyme that are probably responsible for this ratedifference.
- The table presents the rates of reaction at specific substrateconcentrations for an enzyme that displays classicalMichaelis-Menten kinetics. Two sets of inhibitor data arealso included. Determine the Km and Vmax for the uninhibitedenzyme.Inhibition of Purine and Pyrimidine Metabolism by Pharmacological Agents Indicate which reactions of purine or pyrimidine metabolism are affected by the inhibitors (a) azaserine, (b) methotrexate, (c) sulfonamides, (d) allopurinol, and (e) 5-fluorouracil.Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
- With a ∆G°´ of -16.7 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 aboveAn enzyme catalysed reaction has a Km of 8 mM and a Vmax of 13 nM.s-1. Use the Michaelis-Menten equation to calculate the reaction velocity when the substrate concentration is 18 mM.ATP is a (+) allosteric effector, and CTP is a (-) allosteric effector of theenzyme ATCase. Both of these heterotropic effectors bind to the regulatorysubunits on ATCase. The substrates of ATCase, aspartate and carbamoylphosphate, bind the enzyme active site with positive cooperativity (i.e.,they exert a “+” homotropic effect on activity). As the concentrations ofthe substrates change from values where [S] ≪ KM to values where [S] issaturating ([S]≫ KM), how will the binding constants for each of the twoallosteric effectors change? In other words, does ATP bind ATCase withhigher affinity when [S] is low or high? Does CTP bind ATCase with higheraffinity when [S] is low or high?
- Calculate KI' of the inhibitor from the information given. All information may not be needed to calculate. K'm = (29Ki+1.45x10^-10)/Ki Vmax = 11.7 µMs-1 Kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM Inhibitor Concentration = 5x10^-12when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.Dehydratase is a PLP-requiring enzyme that catalyzes an a,b-elimination reaction. Propose a mechanism for this reaction. dehydratasePLP +NH3O OO O− HO O− + NH4