ZuoTi.Pro
Question

3. The enzyme that catalyzes the hydration of CO2 to H2CO3 has a Km = 12...

3. The enzyme that catalyzes the hydration of CO2 to H2CO3 has a Km = 12 mM and a initial speed of 4.5 micromol formed of H2CO3 / mL per second when [CO2] = 36 mM.

a) What is vmax for this enzyme?

b) Assuming that 5 pmol / mL (5 x 10-12 mol / mL) of the enzyme was used in the experiment, what is kcat for the enzyme?

c) What is the catalytic efficiency of the enzyme?

d) Does this enzyme approach “catalytic perfection?
science   biology   
0 0
Add a comment Improve this question Transcribed image text
Next > < Previous
Sort answers by oldest

Homework Answers

Answer #1

Please rate.

0 0
Add a comment
Know the answer?
Add Answer to:
3. The enzyme that catalyzes the hydration of CO2 to H2CO3 has a Km = 12...
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. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions

  • 3) (10 marks) Acetylcholinesterase catalyzes the hydrolysis of the neurotransmitter acetylcholine: Acetylcholine + H2O → acetate...

    3) (10 marks) Acetylcholinesterase catalyzes the hydrolysis of the neurotransmitter acetylcholine: Acetylcholine + H2O → acetate + choline The Km of acetylcholinesterase for its substrate acetylcholine is 9.5x10-5M. In a reaction mixture contain 5 nanomoles/mL of acetylcholinesterase and 150uM acetylcholine, a velocity Ve=40umol/mLsec was observed for the acetylcholinesterase reaction. a. Calculate Vmax for this amount of enzyme b. Calculate kcat for acetylcholinesterase Calculate the catalytic efficiency (kcat/Km) for acetylcholinesterase d. Does acetylcholinesterase approach catalytic perfection? e. What determines the ultimate...

  • The enzyme that hydrolyzes acetylcholine to form acetate and choline has a Km = 9 x...

    The enzyme that hydrolyzes acetylcholine to form acetate and choline has a Km = 9 x 10-5 M for the substrate. In an reaction flask with 5 nanomol / mL of the enzyme and 150 µM of acetylcholine, an initial reaction rate of 40 µmol / mLs was observed. a) Calculate vmax for this amount of enzyme. b) Calculate kcat for the enzyme. c) Calculate the catalytic efficiency of the enzyme. d) Does this enzyme approach “catalytic perfection?

  • The enzyme carbonic anhydrase catalyzes the hydration of CO2 gas in red blood cells:                             &

    The enzyme carbonic anhydrase catalyzes the hydration of CO2 gas in red blood cells:                                                                 CO2 (g) + H2O (L) →H2CO3 (aq) Determine the ∆Ssys of this reaction at 37 °C (body temperature), and justify the sign. *Thermodynamic parameters at T=298K and 1 bar Sm (JK-1 mol-1) Cp (JK-1 MOL-1) CO2 (g) 213.7 36.8 H2O (L) 69.9 78.2 H2CO3 (aq) 187.4 19.4

  • 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...

    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...

  • 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...

  • 12)Show work step by step 13)Show work step by step Below is BoX 6-1 if needed...

    12)Show work step by step 13)Show work step by step Below is BoX 6-1 if needed Applying the Michaelis-Menten Equation IV An enzyme is found that catalyzes the reaction X= Y Researchers find that the Kyn for the substrate A is 4 pm, and the keat is 20 min . (a) In an experiment, (X) = 6 mm, and the initial velocity, V, was 480 nm min!. What was the (E) used in the experiment? (b) In another experiment, (E)...

  • An enzyme has a Km for substrate of 10 mM and Vmax of 5 mol L-1...

    An enzyme has a Km for substrate of 10 mM and Vmax of 5 mol L-1 sec-1 at a total enzyme concentration of 1 nM. At [S] = 10 mM, kcat is: A) 2500 per M per sec. B) 5000 per M per sec. C) 1250 per M per sec. D) 2500 per sec. E) 5000 per sec.

  • 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)...

  • Catalase (MW250,000Da) has one of the highest turnover numbers we know of. It catalyzes the decomposition...

    Catalase (MW250,000Da) has one of the highest turnover numbers we know of. It catalyzes the decomposition of hydrogen peroxide as shown in the reaction                                     (2H2O2à2H2O + O2) If 15.0 mg of pure catalasecatalyzes the decomposition of 0.40 g of H2O2in 1 min at 37 °C at its Vmax, what is the turnover number (kcat) of catalase(in units of sec-1)? Plot a graph of Abs vs. time at different concentrations of enzyme and replot a figure and find out the optimal...

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