Initial rates of an enzyme-catalyzed reaction for various substrate concentrations are listed in the table below....
s- (3 pts) The flowing rates have been an enzyme- catalyzed reaction at various substrate concentrations: Run no. 103 [S]M Rate, v/ (Ms') 2.41 3.33 4.78 6.17 7.41 9.52 0.0 12.5 0.4 0.6 4 2.0 4.0 a- From Line-Weaver double reciprocal plot, obtain and Mechaelis-Menten constant, max b- If the enzyme concentration is 1.00 x 10-11 M calculate kz.
10.11 The initial rates at various substra tions for an enzyme-catalyzed reaction are ious substrate concentra ed reaction are as follows: Vo/10-6 M min-1 38.0 53.4 S/M 2.5 x 10-5 4.00 x 10-5 6.00 x 10-5 8.00 x 10-5 16.0 x 10-5 20.0 x 10-5 68.6 80.0 106.8 114.0 (a) Does this reaction follow Michaelis-Menten kinet- ics? (b) Calculate the value of V max of the reaction. (c) Calculate the K value of the
The initial rate, V, of an enzyme catalyzed reaction varies with substrate concentration as follows: 106 x Initial rate, Ms SJ, M 0.020 0.585 0.004 0.495 0.002 0.392 0.001 0.312 0.250 0.00066 Determine Vmax and Km for this reaction
The following data has been obtained for an enzyme-catalyzed reaction with two different initial enzyme concentrations of 0.025g/L and 0.015g/L. V (g/L.min) [S] (g/L) Eo = 0.025g/L Ep = 0.015g/L 56.8 1.75 1.05 28.4 1.58 0.97 19.1 1.47 0.89 14.3 1.38 0.83 11.4 1.31 0.77 9.4 1.22 0.73 8.2 1.15 0.69 7.1 1.08 0.66 (a) Using the Lineweaver-Burke plot, determine Km and Vm for Eo = 0.025g/L (b) Using the Lineweaver-Burke plot, determine Km and Vm for Ep = 0.015g/L...
Under what circumstances does an enzyme catalyzed reaction rate resemble a non-enzyme catalyzed reaction? At very low concentrations of substrate (Km is greater than S) the Michaelis-Menton equation can be simplified to? At very high concentrations of substrate, the Michaelis-Menton equation can be simplified to? How do you determine the initial rate of reaction
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K? Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
At high (saturating) substrate concentrations, the rate of an enzyme-catalyzed reaction approaches Vmax. How close does the reaction rate actually get to Vmax? Determine how high (i.e. how many times Km) the substrate concentration must be for the reaction rate to be: a. 98% Vmax (show your work) (2) b. 99% Vmax (answer only) (1) c. 99.9% Vmax (answer only) (1)
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....