The enzyme catalase catalyzes the decomposition of hydrogen
peroxide. The following data are obtained regarding the rate of
reaction as a function of substrate concentration using
concentration of catalase equals to 3.5 x 10^–9 M : Analyzing the
data using the Lineweaver-Burk plot:
we calculated the S = 0.698 s , and I = 26.6 M^-1 s , Km for this enzyme is:
Solution :
Given that
The enzyme catalase catalyzes the decomposition of hydrogen peroxide. The following data are obtained regarding the rate of reaction as a function of substrate concentration using concentration of ca...
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
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
need B C and D done please please please help!!! 1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A, she determined that ?m=2.5 μM and ?cat=35 min−1. Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows Michaelis–Menten kinetics. 1)...
An enzyme catalyzes the reaction A ® B. The initial rate of the reaction was measured as a function of the concentration of A (substrate). The following data were obtained: [10 pts.] [A], micromolar V0, nmoles/min 0.05 0.08 0.1 0.16 0.5 0.79 1 1.6 5 7.3 10 13 50 40 100 53 500 73 1,000 76 5,000 79 10,000 80 20,000 80 Answer the following questions: What...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate A, she determined 30 min that Km 3.0 HM and kcat Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows...
1) 2) If the total enzyme concentration was 9 nmol/Lnmol/L, how many molecules of substrate can a molecule of enzyme process in each minute? Express your answer to three significant figures. 3) The kcat for neuraminidase at pH=6.15pH=6.15, 37 ∘C∘C is 26.8 s−1s−1. Calculate KMKM for the hydrolysis of sialic acid. Express your answer with the appropriate units. An enzyme that follows Michaelis-Menten kinetics has a Ky value of 6.00 uM and a keat value of 176 s-1. At an...
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50 x 10 1.00 x 10-4 1.00 x 10-3 Reaction velocity (nM/min) 15 56 60 75 (1) Estimate Km and Vmax- (2) What would V be at S=2.5 x 10-5 ?
The decomposition of hydrogen peroxide at 200 °C involves a first order rate law. The starting concentration of H202 is 0.20 M and changes to 0.0050 M after 10 minutes. Calculate the rate constant (in s1). 2H202(aq) 2H20(I) + 02(g) Select one: a. 4.0x 10-3 b. 4.0x 10-4 c. 6.1 x 103 d. 6.1 x 10-2 e. 4.0 x 10-2
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.