HAPPY ↔ SAD
You begin devising ways to characterize the enzyme. (5 points total, 2 each for A, B and 1 for C).
Enzyme kinetics: You recently joined a new research group, and in your first week you successfully...
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....
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD Previously, you determined that kcat = 400 s and Km = 10 M for your sample of happyase. Further research shows that this happyase sample was actually contaminated with a reversible inhibitor called ANGER. When ANGER is fully removed from the happyase preparation and [Eltotalis 4 nM, the measured Vmax is increased to 4.8 umes-1 and the measured Km is now 15 MM. Use...
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...
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...
. 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...
10.What type of inhibitor is this? How do you know? (2)
11.For your assigned inhibitor 1, what are the apparent Km &
Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in
presence of inhibitor, at a given concentration.) (2)
Kinetics experiments were performed on PGI. Enzyme activity
(initial velocity, Vo) was measured at varying concentrations of
Glucose-6-phosphate (G6P). The enzyme concentration used in all
experiments was 1.5 μM.
12.What will be the reaction rate with 0.500 mM...
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...
Applying the Michaelis-Menten Equation II Another enzyme is found that catalyzes the reaction A <===> B Researchers find that the K for the substrate A is 4 uM, and the kcat is 20 min^-1 (a) In an experiment, [A] = 6 mM, and the initial velocity, Vo was 480 nM min^-1 What was the [Et] used in the experiment? (b) In another experiment, [Et] 0.5uM, and the measured Vo=5uM min^-1 What was the [A] used in the experiment? ( c)...
1) An experiment is run with enzyme E at a constant concentration of 1.00 nM. The following data set was generated: Initial rate v, [SJ, μΜ μΜ/min 2.0 2.9 3.0 3.8 4.0 4.4 5.0 5.0 5.4 6.0 7.0 5.8 8.0 6.2 9.0 6.4 6.7 10.0 From these data, determine Vmax, KM, kcat and the turnover number. In a second series of experiment, the reaction was studied in the presence of 10mM of inhibitor A. The new data set is shown...
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)...