The following kinetic data were obtained for an enzyme in the absence of an inhibitor (1) and in the presence of two different inhibitors (2) and (3) at 5mM concentration.   [S], mM (mmol/mL/sec) (mmol/mL/sec) (mmol/mL/sec)   (1) (2) (3) 1 12 4.3 5.5 2 20 8 9 3 29 14 13 8 35 21 16 12 40 26 18   Determine the Vmax and KM of the enzyme Determine the type of inhibition.

For an enzyme kinetics experiment, a student prepared a reaction mixture by mixing 450 microliters of 0.75mM PNPP with 4.25ml of 0.2M Tris-HCl buffer. When he is ready to measure the absorbance, he added 0.3ml of Alkaline Phosphatase to the mixture and mixed thoroughly. What is the substrate concentration at the beginning of the reaction in mM ?

You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?

Describe reaction between AP and PNPP and how is used to determine the kinetic parameters of AP. i. İndicate the value for the activity of AP(which is 3.08) What does it mean? Is your enzyme active or not? What does it say about the purity of your enzyme? ii. How the purification process affects the activity?

The glucose oxidase used in this experiment has a concentration of 27 U/mg. Calculate the mass (in g) of solid glucose oxidase required to react with all the glucose in 4.00 µL of10.0- mM glucose sample assuming the reaction proceeds for 30 minutes.

You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM

The following data have been obtained for two different initial enzyme concentrations for an enzyme-catalyzed reaction. [E]=0.015 g/l) (g/l-min) [S] (g/l) v([E]=0.00875 g/l) (g/l-min) 1.14 20.0 0.67 0.87 10.0 0.51 0.70 6.7 0.41 0.59 5.0 0.34 0.50 4.0 0.29 0.44 3.3 0.39 2.9 0.35 2.5 a. Find K b. Find V for [E]=0.015 g/l. c. Find V for [E]=0.00875 g/l. d. Find k2. Use Eddie-Hostee plot to find your answer. Compare your result using Hanes- Wolf plot.

Explain how running a reaction with the enzyme aldolase at a pH of 14 affects its activity Enzyme Activity e Activity 765432TO Factors Affecting Enzyme Activity 0 6543 2 6 Solution pH 8 a) It significantly diminishes activity because enzyme is denatured b) It significantly diminishes activity because the enzyme becomes too reactive Oc) It will quadruple its activity because enzyme is denatured and free Question 9 (5 points) Estimate the optimum pH required for maximum enzyme activity 10 d) It will double its activity because enzyme now has more active sites 12 Factors Affecting Enzyme Activity