111 The Michaelis constant is represented by what variable, and is comprised of which rate constants in the overa enzyme rate equation? e. Km, kf, k, and k_cat f. Vmax, kf and kcat g. Km, kf, k, and kcat h. Vmax, kf, kr, and kcat i. Km, kf and kcat
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- Locate the point of saturation. choices: a,b,c At what point where the addition of substrate results to the increase of rate of enzymatic activity? choices: a to b, b to c, a to c The graph shows that enzymatic activity is directly proportional to substrate concentration from point A to C. choices: agree or disagreeSolve the Michaelis-Menten equation for KM when vo=Vmax/2. What does this tell you about the relationship between substrate concentration and enzymes with high KM values? With low KM values?2. The enzymatic reaction rate r is given by equation 2 below as a function of substrate concentration Cs and kinetics parameters KM and rmax. Using linear and nonlinear regression in excel, evaluate the kinetic parameter constants of a biosystem given the gathered data from a series of batch runs
- 47. Which of the following is true under the following conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 mM. (1 nM = 10-9 M, 1 μM=10-6 M, 1 mM = 10-3 M) Group of answer choices Between 0% and 50% of active sites have substrate bound 0% of active sites have substrate bound 50% of active sites have substrate bound 100% of active sites have substrate bound Between 50% and 100% of active sites have substrate boundBased on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the substrate into product? A) Vmax = 10 uM s-1, KM = 10 µM B) Vmax = 10 uM s-1, KM = 0.01 µM C) Vmax = 1000 uM s-1, KM = 500 µM D) Vmax = 1 uM s-1, KM = 1 µM E) Vmax = 200 uM s-1, KM = 10 µMList four (4) individual alloantibodies which react preferentially at room temp or below.
- Calculate the Vmax of the above enzyme (lactase). (the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 mM per minute 0.25 mM per minute 0.50 mM per minute 1.25 mM per minute 5.0 mM per minuteWhat enzyme kinetic parameters are apparently impacted by competitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor VmaxBy whom the 10% energy transfer law of food chain was given?
- Match each inhibitor with its effect on Michaelis-Menten reactions. Group of answer choices Vmax and apparent Vmax are equal and the apparent Km is greater than Km. The apparent Vmax is less than Vmax and the apparent Km and Km are equal The apparent Vmax and the apparent Km are both lowered to the same degree. The apparent Vmax is less than Vmax and the apparent Km can be either greater than or less than Km.Part a) Which graph has the largest kcat? Please explain. Part b) Which graph has the tightest substrate binding? Please explain. Part c) Which graph has the largest specificity or efficiency constant? Please explain.A biochemst wants to dtermine the effect of inhibitor on a certain enzyme. See attached data. Using linaer regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. Km Using linear regression analysis determine the values of Vmax and Km of the enzyme in the presence of inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. Km