You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD...
. ous enzyme 'happyase catalyzes t the conversion of SAD to HAPPY with a Keat 100 sec 40 35 30 25 20 10 10 20 30 40 50 60 70 90 100 110 ISADI QIM A kinetic experiment was conducted and the intitial velocity of the reaction as a function of SAD concentration is shown above. The initial velocity at 1 mM [SAD] was measured to be 40 nM/sec. a) What is the total [happyase] used above (make sure to...
Question 13 of 49 A research group discovers a new version of happyase, which they call happyase,that catalyzes the chemical reaction Map HAPPYSAD The researchers begin to characterize the enzyme a In the first experiment, with [El at 6 nM, they find that the Vmax is 3.50 Ms Based on this experiment, what is the keat for happyase ? In another experiment, with [E] at 3 nM and [HAPPY] at 40 HM, the researchers find that Vo 1390 nM s1....
Enzyme kinetics: You recently joined a new research group, and in your first week you successfully discover a new version of an enzyme called happyase, which you name happyase*, that catalyzes the chemical reaction: HAPPY ↔ SAD You begin devising ways to characterize the enzyme. (5 points total, 2 each for A, B and 1 for C). In the first experiment, with [Et] at 4 nM, you find that the Vmax is 1.6 mM/s. Based on this experiment, what is...
QUESTION 3 The enzyme happyase catalyzes the following reaction: SAD = HAPPY An enzyme kinetics experiment gave the data shown in the table below. The concentration of happyase used in the experiment was 25.00 UM. [SAD] (MM) 1.000 2.000 3.000 4.000 Vo (mm/s) 3.700 6.727 9.250 11.385 Determine the value of Vmax for happyase (in mM/s). QUESTION 4 Using the information above, determine the value of Km for happyase (in mm). QUESTION 5 How long (in milliseconds) does a single...
An enzyme catalyzes the reaction M↽−−⇀N . An enzyme catalyzes the reaction M = N. The enzyme is present at a concentration of 3.5 nM, and the Vmax is 1.9 uM -. The Km for substrate M is 2.9 uM. Calculate kcat kcat = 542.86 What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an a' of 1.5? apparent Vmax = 0.526 UM s-1 apparent Km = 1.2
An enzyme catalyzes the reaction M N. The enzyme is present at a concentration of 3.5 nM, and the Vmax is 2.9 PM s-. The Km for substrate M is 6.5 MM. Calculate kcat kcat = 1 What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an a' of 1.3? apparent Vmax = UM S-1 apparent Km = UM
Question 1 (2 points, 1 point for each correct answer) A research group discovered a new enzyme happyase that catalyzes chemical reaction SAD STUDENT HAPPY STUDENT Researchers characterized this enzyme and found that at [E,-10 nM this enzyme has Vmax at 2.5 μM/s. It was also experimentally measured that at [SAD STUDENT)-0.05 mM this enzyme has Vo -500 nM/s. What are the kat and Km of the happyase enzyme? Make sure to write down units of measure! Answers: keat- Question...
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...
11. In Excel, prepare Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available: V, umol/min umol/min (No Inhibitor) S], mM (Inhibitor Present) 3.66 5.12 6.18 6.98 7.60 4.58 6.40 7.72 8.72 9.50 3.0 5.0 7.0 9.0 11.0 a. What are the KM and Vmax values for the inhibited and uninhibited reaction 5 pts. each reaction) b. Is the inhibitor competitive or noncompetitive? (5 pts.) Micheli-Menten) EQUATIONS: VV
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)...