The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] U = Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. 300 V Next, move the line labeled 1/2 Vmax to its correct position. max 275 Then, move the line labeled Km to its correct position. 250 225 200 175 Michaelis–Menten curve 150 K a 125 m 100 1/2 V 75 max 50 25 10 20 30 40 50 60 70 80 90 100 [S] (µM) Incorrect Estimate the values for Vmax and Km. Vmax 175 µM/min Km 14 µM v (µM/min)

The enzyme examase catalyses the following reaction, A - B where A is the reactant and B is the product A595 measurements were used to determine the catalytic activity of examase by measuring the rate at which B is produced. From this, the activity of the enzyme was determined to be 42 µmol/mL per minute. A standard albumin solution (concentration = 10 mg/mL) was used to prepare a standard curve of Abs595 vs amount of protein in mg. The protein assay was also performed using 100 uL of a 1 in 10 dilution of the original examase sample. For the absorbance measurements, it was determined that the sample used in the A595 measurement contains 1.2 mg of examase. Which of the following statements correctly gives the specific activity of examase? 1.0.35 U/mg O 2.0.035 U/mg 3. 5040 U/mg O 4.35 U/mg O 5.3.5 U/mg

what is the activation energy? rate = r = k [I-]^1 [S2O82-]^1 Mixtures:             Temperatures (celsius):        Initial Rates: 1                                      21.9                               6.45 * 10-4 2                                     38.9                              3.54 * 10-4 3                                      2.4                               4.35 * 10-4

The recombination reaction2 HO2(g) → H2O2(g) + O2(g)has a second-order rate constant of 2E9 M-1 s-1. Calculate the half-life of the reaction if the initial concentration of HO2(g) is 2.58E-11 M.Note: the coefficient 2 in the reaction means that the integrated rate law for this reaction is:1/ct = 1/c0 + 2kt

Temperature effect on the degradation of a multisulfa preparation was evaluated at 60 and 70°C. If the first-order reaction rate constants responsible for the degradation at these two temperatures were 8.2 x 10-4 and 1.96 x 10-3 hr-1, respectively, answer the following TWO questions.   Calculate the frequency factor, A, for the degradation of this drug within this temperature range (in hr-1).

Attached is the basic model for an enzyme-catalyzed reaction. Assume that substrate binding is rate determining. Write the equations for the total amount of enzyme in the reaction and the rate of the reaction. Is A or B correct? If not, show work for the correct answer A :  [E] = [ES] + E  B :  [E] = [E]0 - [ES] ; r= k2 [E]0 S / kM + [E]