Question

For the following lines calculate the Vmax, Km, Ki, and inhibitor concentration. T he double reciprocal...

For the following lines calculate the Vmax, Km, Ki, and inhibitor concentration. T

he double reciprocal plot equations:

Enzyme y=.0044x+.0035

Enzyme + inhibitor y=.0088x+.0079

Science   Chemistry   
0 0
Add a commentTranscribed image text
Next >

Homework Answers

Answer #1

0 0
Know the answer?
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Log In

Sign Up

Not the answer you're looking for?
Ask your own homework help question
Similar Questions
a) The Km of an enzyme of an enzyme-catalyzed reaction is 7.5 µM. What substrate concentration...
a) The Km of an enzyme of an enzyme-catalyzed reaction is 7.5 µM. What substrate concentration will be required to obtain 65% of Vmax for this enzyme? (same enzyme was used in part a and b) b) Calculate the Ki for a competitive inhibitor whose concentration is 7 x10-6 M. The Km in the presence of inhibitor was found to be 1.2x10-5 M. 
An experimenter performs two sets of enzyme kinetics experiments. One set of experiments, when plotted as...
An experimenter performs two sets of enzyme kinetics experiments. One set of experiments, when plotted as a double-reciprocal plot, yielded a y-intercept of 0.043 μM-1·min and an x-intercept of -20.0 mM-1. A second set of experiments, when similarly plotted, yielded a y-intercept of 0.129 μM-1·min and an x-intercept of -60.0 mM-1. The second set of experiments contained 75 nM of an uncompetitive inhibitor. Given these data, what is the Ki' (in nM to the nearest tenths) for this inhibitor? Hint:...
An enzyme follows Michaelis-Menten kinetics. How does the following things affect the Km and the Vmax....
An enzyme follows Michaelis-Menten kinetics. How does the following things affect the Km and the Vmax. Explain how they are affected and why. 1. A competitive inhibitor 2. A Mixed inhibitor 3. 6 M urea 4. doubling [S]
Enzyme Kinetics: Plot the data below and calculate the kinetic parameters, Km and Vmax. You must...
Enzyme Kinetics: Plot the data below and calculate the kinetic parameters, Km and Vmax. You must submit the graph with your calculated parameters [S] (uM) 0.1, 0.2, 0.4, 0.8, 1.6 vo (mM/s) 0.34, 0.53, 0.74, 0.91, 1.04
The following parameter(s) of an enzyme-catalyzed reaction depend(s) on enzyme concentration: A) Km (Michaelis constant) B)...
The following parameter(s) of an enzyme-catalyzed reaction depend(s) on enzyme concentration: A) Km (Michaelis constant) B) Vmax (maximum velocity) C) kcat (turnover number) D) A and B E) B and C Km is the equivalent of: A) Substrate concentration at Vo B) Substrate concentration when Vmax is reached C) Substrate concentration when 1/2 Vmax is reached D) Product concentration when 1/2 Vmax is reached
Calculate vi and the degree of inhibition caused by a competitive inhibitor under the following conditions:...
Calculate vi and the degree of inhibition caused by a competitive inhibitor under the following conditions: (a) [S] = 2x10-5 M and [I] = 2x10-3 M, (b) [S] = 4x10-4 M and [I] = 2x10-3 ​M, and (c) [S] = 7.5x10-3 M and [I] = 10-5 M. Assume that Km = 2x10-3 M, Ki = 1.5x10-4 M, and Vmax = 270 nmoles/Lxmin.
Which of the following in not true for an enzymatic reaction that shows Michaelis-Menten kinetics? Group...
Which of the following in not true for an enzymatic reaction that shows Michaelis-Menten kinetics? Group of answer choices the rate steadily decreases over the course of the reaction Vmax depends on the concentration of the enzyme in the presence of an inhibitor the v vs. [S] plot is a hyperbola the equilibrium constant is lower as compared to the uncatalyzed reaction KM is determined by finding the [S] at which v = Vmax/2
Use the following information and the equation of the line y = 1.00 x 104x +...
Use the following information and the equation of the line y = 1.00 x 104x + 135 to find the Vmax, Km, kcat, and Km. Include proper units. In a test of a certain inhibition enzyme, a scientist used 0, 35.0 nM and 75.0 nM of the inhibitor in a 1.00 mL assay volume, she added 23.78 mg of the enzyme, which as a molecular weight of 58.0 kD. The rates were measured in mM/min and the substrate concentrations were...
Your labmate is studying the kinetics of the enzyme Pyruvate kinase with its substrate phosphoenolpyruvate (PEP),...
Your labmate is studying the kinetics of the enzyme Pyruvate kinase with its substrate phosphoenolpyruvate (PEP), and has obtained the following results. When performing reactions with 0.2 nM Pyruvate Kinase, he measured the Km and Vmax and found that they equal 0.5 mM and 20 mM/s, respectively.  Draw a double-reciprocal (Lineweaver-Burke) plot for these data; be sure to label the axes with names, units, and values.
(a) Sequencing the genome of a newly identified virus gave the following base composition: A =...
(a) Sequencing the genome of a newly identified virus gave the following base composition: A = 33%, G = 33%, C = 17%, and T = 17%. The results suggest that this is a ____________ virus. Group of answer choices single-stranded RNA double-stranded RNA double-stranded DNA single-stranded DNA double-stranded RNA:DNA (b) The activity of a protein is close to zero at pH = 4 and below, high at pH 8 and above. The activity of this protein probably depends upon...
ADVERTISEMENT
Need Online Homework Help?

Get Answers For Free
Most questions answered within 1 hours.

Ask a Question
ADVERTISEMENT