A penicillinase inactivates a penicillin. An enzyme with Mw = 30,000 has only a single active site, kcat = 2,000 s-1 and KM = 5.10-5 M. In response to a treatment with 5 μmol of penicillin, a 1 mL suspension of bacteria releases 0, 5 µg of enzyme. A) What concentration of penicillin would cause the enzyme to react at half the maximum rate? B) A modified penicillin acts as a competitive inhibitor. If the affinity of E for penicillin and for modified penicillin are the same, what concentration of inhibitor reduces the rate of penicillin loss 5-fold with low Cs in the medium?

Q: An enzyme has a Km equal to 1.0 x 10-4 M (molar) for a certain substrate S. When [S] = 1.0 x 10-4 M,…

A: Km = 1.0 x 10-4 M [S] = 1.0 x 10-4 M     Vo = Vmax[S]/{Km + [S]} At Km = [S] Vo = Vmax/2   (a) and…

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A: Calculation of Kb: Kb=vmax[E]0=0.250 mmol dm-3 s-12.3×10-6 mmol dm-3=0.11×106 s-1

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Q: 1. Initial rates of enzyme-catalyzed reaction for various substrate concentrations are listed below:…

A: Rate(V) mol/(L.min)*106 Substrate concentration (s) (mol/L (1/v)*10-6 1/s 177 0.0041 0.00565…

Q: please answer this :)

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Q: For the attachment of a substrate to the active site of an enzyme: k1 S+E→ SE k-1 The equilibrium…

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Q: E17F.5(b) The enzyme-catalysed conversion of a substrate at 298 K has K 0.032mol dm and 425x10 mol…

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Q: For the following reaction catalysed by an enzyme E k1 E + S = ES k-1 E + P • describe the meaning…

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Q: 7. Consider the following mechanism and reaction coordinate diagram. Step 1: A(g) + B(g) → AB(g) 60…

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Q: The following initial rate data were obtained on the rate of binding of glucose with the enzyme…

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Q: The following data were obtained in a study of the rate of inversion ofsucrose at 25 °C. The initial…

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Q: 25. A student measures the following initial rate data for an enzyme that obeys Michaelis- Menten…

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Q: 3. Enzyme kinetics. The reaction in question 3 is catalyzed by an enzyme called triose phosphate…

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Q: 7°C, the rate constant is 4.90 × 10-4 min-1. At 39°C, the rate constant is 0.00139 min-1. By what…

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Q: 10.38. The following data relate to an enzyme reaction. 10³[S]/mol dm³ 105 V/mol dm³ s-1 2.0 13 4.0…

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Q: The rote of the reaction between hemoglobin (Hb) and carbon monoxide (CO) was studied at 20°C. The…

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Q: Step by step please

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Q: E17F.5(b) The enzyme-catalysed conversion of a substrate at 298K has K 0.032mol dm and concentration…

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Q: Given the following initial rate data, calculate the specific rate constant. Experiment [A]o, M…

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Q: The following data were obtained for the reaction A + B + C⟶⟶ products:     Expt #   [A]0…

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Q: P17B.3 The data below apply to the formation of urea from ammonium cyanate, NH CNO NH,CONH.…

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Q: The enzyme-catalyzed conversion of .1 a substrate at 250C has a Km of 0.035M. The rate of the -1…

A: Given: KM = 0.035 M Vo = 1.15x10-3 M.s-1 [S] = 0.110 M

Q: 15. Consider an enzyme that has a kcat that is 1000.0 times larger than kuncat at 15°C. If the…

A: T = 15°C  Or T = 15+273 = 288 K  16.5 KJ/mol enzyme decreases the activation energy for the…