Question
Please do everything like you were answering a test. Don’t attempt if youre not going to do all parts. Do it ASAP and I will give you a good rating. If not I will report you. Thank you so much for being the best. Show work if necessary and be concise. There’s no way for me to separate so do all parts.

2. i) (10 points) The enzyme A catalyzes the hydrolysis of the peptide A-G-W in 10mM phosphate buffer at pH 4. Assuming thi

points) An inhibitor T was added to the reaction mixture. The Vmas measured was 800mMol/min olmin and the KM-2.5 mM. What t

do all parts please. I cant seperate it because it will be refunded.
2. i) (10 points) The enzyme "A" catalyzes the hydrolysis of the peptide A-G-W in 10mM phosphate buffer at pH 4. Assuming this enzyme follows Michaelis-Menten kinetics, calculate the Vmax of the enzyme if KM 3mM, Vo 150mMol/min and [S]-0.5mM. i) (5 points) What is the initial velocity of the enzyme catalyzed reaction as a percentage of Vmax, if [S] 1.5 KM
points) An inhibitor "T" was added to the reaction mixture. The Vmas measured was 800mMol/min olmin and the KM-2.5 mM. What type of an inhibitor was it? V)(extra credit) For the same reaction in question iii, if the y intercept of the graph in the for that presence of 1mM of inhibitor was given by (+VI) Vmax,, calculate K inhibitor. V) (5 points) Sketch the Lineweaver-Burk plot in the presence and in the absence of an inhibitor? Label axes, curves, important intercepts, slopes.
0 0
Add a comment Improve this question Transcribed image text
Answer #1

km (1 enat oven in probl Compart t uwe qeh Lind tweaver Bunk pat . ) is1 eplKi ki S o j)啤inhibitor laddad use-tion we.find that serun个bd usin.1 km

Add a comment
Know the answer?
Add Answer to:
Please do everything like you were answering a test. Don’t attempt if youre not going to do all p...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for? Ask your own homework help question. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions
  • Please show me how to solve these and I'll give thumbs up. Thank you! Question 6...

    Please show me how to solve these and I'll give thumbs up. Thank you! Question 6 O out of 10 points An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with X- intercepts of -10mM -1 and -3.5mM-1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? Question 7 O...

  • 112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the...

    112 marks] 3. The relationship between initial velocity (V.) and substrate concentration of most of the enzyme- catalized reactions are explained by Michaelis-Menten equation. IMPORTANT: Show the calculations and indicate the units for all your answers. a. For an enzyme which follows the Michaelis-Menten enzyme kinetics, Km is 50 mmol L. Calculate the substrate concentration required to obtain the initial velocity (V.) equivalent to 90% of the maximum velocity (Vmax). b. The Vmax of the above reaction is 250 mmol...

  • (I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk...

    (I need help with part C, Drawing the expected Michaelis-Menten plot; Do NOT draw the Lineweaver-Burk plot. thanks!) 1. Michaelis-Menten kinetics- use the M-M equation to answer the following: a. An enzyme (5 µM) has a Vmax of 450 mM/min. What is kcat? b. When the substrate concentration is 50 mM, the initial velocity (V0) was measured to be 375 mM/min. Under the conditions described above, calculate the KM. c. Draw the expected Michaelis-Menten plot (label your axes and include...

  • 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...

  • The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equatio...

    The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...

  • need B C and D done please please please help!!! 1. You measure the initial rate...

    need B C and D done please please please help!!! 1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...

  • 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...

  • Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bo...

    Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...

  • 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP...

    30. Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Sphingosine (UM)v. (mg/min) v. (mg/min) with inhibitor 2.5 32.3 8.5 3.5 40 11.5 50.8 14.6 25.4 87.7 43.9 115.4 70.8 Construct a Lineweaver-Burk plot to answer the following...

  • Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The...

    Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Sphingosine (uM) vo (mg /min) vo (mg /min) with inhibitor 2.5 32.3 8.5 3.5 40 11.5 5.0 50.8 14.6 10 72...

ADVERTISEMENT
Free Homework Help App
Download From Google Play
Scan Your Homework
to Get Instant Free Answers
Need Online Homework Help?
Ask a Question
Get Answers For Free
Most questions answered within 3 hours.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT