For the reaction E + S <> ES, what is the [E] if [S] = 0.18 mM, [ES] = 133 uM, and the Kd = 15 uM? 11,000 UM 20 uM 11 uM 180 uM
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- In your acid phosphatase enzyme kinetics lab, you constructed a Lineweaver-Burk plot. Lefs assume that you graphicaly obtain 1/Vmax - 9.33 (umoliey and -1Km--0.012 M. Which of the following is correct? A) Vmax = 9.33 (no units) B) Km = 0.012 (no units) C) Vmax = (1/Vru" = 0.107 umolis D) Km =-14-1K = 83.3 pM E) Both C) and D) are correctPlease note the following Lineweaver-Burk plot for the enzyme Virbraniumase reacting with a substrate: -0.4 . 1/V 5 4 3 2 -0.2 0 0.2 y = 5.2781x + 1.3338 R² = 0.9967 0.4 0.6 0.8 1/[S] 1 Based on the information provided, what is the Vmax for this reaction?An enzyme has the following values: vmax's; 0.028 M s-' and 0.021 M s-' (I), and km's; 0.00198 M and 0.00197 M (I), when the total concentration of enzyme is 10-º M. The (I) values were determined with 1 microM inhibitor. Select the value closest to the k, for this enzyme. (hint 1 microM = 10-6 M).
- The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.From a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.A Lineweaver-Burk plot generates a line with the following formula: y = 0.3x + 0.4. What is the Km of this enzyme?
- Suppose the biochemical pathway represented in Equation 5-10a is coupled at its first step to the hydrolysis of ATP to ADP. How would this change the expres- sion for AG of the pathway?1. A Lineweaver-Burk Plot is shown below. 30 25 Curve A y = 3.1207x + 2.4978 20 15 Curve B y = 1.0003x + 2.3602 10 5 -3 1 5 7 11 1/[Catechol] (mM1) With these curves, determine the following enzyme parameters. Show all pertinent solutions. a. Km of Curve A and Curve B b. Vmax of Curve A and Curve B c. Assuming that one of these curves corresponds to the kinetics of one enzyme and one substrate, which curve represents the effect of an inhibitor? Why do you say so? d. What type of inhibition is exhibited by your answer in question c? Why do you say so? 1/V, (units of activity 1)If a data from an enzyme experiment is plotted as a Lineweaver - Burk plot, and the Vmax is 0.02 sec/mol, and x-intercept is -2.5 mM-1, then what is the KM value?
- From a kinetics experiment, kcat was determined to be 295sec-1. For the kinetic assay, 0.3mL of a 0.25mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 3mL. Calculate Vmax (µM∙min-1) for the enzyme and catalytic efficiency ( in M-1sec-1) for the enzyme. The Km for the enzyme was determined to be 2.55 x 10-2M.Use the concept of Hess' Law to determine AH for the process V 2X +Z given the following numbered processes: V 2 W AH1 W X + Y AH2 Z- 2Y AH3 ΔΗ+ ΔH +ΔΗ3 ΟΔΗ+ 2ΔΗ-ΔΗ3 ΟΔΗ+ 2ΔΗ2+ ΔΗ3 ΔΗ + ΔH,-ΔΗ3What is the likely keq for an enzyme that has a deltaG =-18.3kj/mol?