46.) Which of the following lists steps of glycolysis that are considered reversible? А) 1, 3, & 7 В) 2, 3, & 9 С) 1, 2, & 7 D) 4, 5, & 6 E) 2, 4, & 10 F) none of the above
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Question #46
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- 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?In the "Catalysis by Preferential Transition State Binding" mechanism, the substrate perfectly fits with the enzyme binding site after its geometry gets changed. Who does it? And how?The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8
- Given an enzyme with KM of 0.5mM, at what substrate concentration will the velocity of the enzyme reach ¼ Vmax. (Vmax-200 mmol/s)A protein catalyzes the following reaction and had a Michaelis-Menten constant of Km=25 mM and a turnover number of 4.0 x 107 s-1. The total enzyme concentration is 0.012 µM and the initial substrate concentration is 4.76 µM. The enzyme has a single active site. Calculate the values of Vmax and V0 for this enzyme. 2H2O2 (aq) -----> 2H2O(l) + O2(g) Vmax= Vo=6. What is the instantaneous reaction rate for an enzyme system? k = 0.087 1/h; enzyme concentration = 0.02 M; substrate concentration = 0.05 M; and Km concentration = 0.01 M? Answer should be in units of mM/h
- Kinetics data were gathered for an enzyme-catalyzed reaction under identical conditions both with and without a noncompetitive inhibitor. When the inhibitor was present at a concentration of 42.2 nM, the value of Vmax decreased by 20.3%. What is the value of Ki for this inhibitor?Relation between Reaction Velocity and Substrate Concentration: Michaelis-Menten Equation. a)At what substrate concentration would an enzyme with a kcatof 30.0 s-1and a Kmof 0.0050 M operate at one-quarter of its maximum rate? b)Determine the fraction of Vmax that would be obtained at the following substrate concentrations [S]:1/2Km,2Km,and10Km. c)An enzyme that catalyzes the reaction X ßàY is isolated from two bacterial species. The enzymes have the same Vmax, but different Km values for the substrate X. Enzyme A has a Km of 2.0 μM, while enzyme B has a Km of 0.5 μM. The plot below shows the kinetics of reactions carried out with the same concentration of each enzyme and with [X]=1 μM. Which curve corresponds to which enzyme?Salicylic acid salts inhibit the catalytic action of a glutamate dehydrogenase. Determine the type of inhibition by graphical analysis of the Following data. Assume that the salicylate concentration remains constant and is 40 mM. Also calculate the KM for the substrate and the dissociation constant for the enzyme-inhibitor complex. [S] mM 1.5 2.0 3.0 4.0 8.0 16.0 Without salicylate Product (mmol/min) 0.21 0.25 0.28 0.33 0.44 0.4 With salicylate Product (mmol/min) 0.08 0.10 0.12 0.13 0.16 0.18
- Estimate KI for a competitive inhibitor when [I] = 5 mM gives an apparent value of KM that is three times the KM for the uninhibited reaction.An enzyme catalyzes a reaction with a KmKm of 7.507.50 mM and a VmaxVmax of 3.00 mM⋅s−1.3.00 mM⋅s−1. Calculate the reaction velocity, v0,v0, for each substrate concentration. a. [S]=4.00mM*s^-1 b. [S]=7.5mM*s^-1An enzyme E binds a substrate S and a cofactor C. The equilibrium dissociation constant Kd,S of the enzyme-substrate complex ES is 1 mM, for EC it is 10 mM. When the cofactor C is present, Kd,s ’ is decreased to 0.1 mM. What is the value for the dissociation constant Kd,C ’ of the enzyme-cofactor complexing the presence of substrate S? Calculate the interaction energy DDGint for cofactor and substrate binding.