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. ous enzyme 'happyase catalyzes t the conversion of SAD to HAPPY with a Keat 100...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD...
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 3 The enzyme happyase catalyzes the following reaction: SAD = HAPPY An enzyme kinetics experiment...
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...
Question 13 of 49 A research group discovers a new version of happyase, which they call...
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...
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...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The...
Question 1 (2 points, 1 point for each correct answer) A research group discovered a new...
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...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate...
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...
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)...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A,...
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)...
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 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...
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....
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...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
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...
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