Question

Isolation of a certain enzyme by two different scientists produce solutions of pure enzyme but with different enzyme concentrations. If measured separately on the two solution which results will be the same? (a) KM (b) Vmax (c) k3

0 0
Add a comment Improve this question Transcribed image text
Answer #1

The answer is- a) KM

The KM will remain same.

We know Km = 1/2 Vmax. The concentration of substrate at which enzyme achieve half V max.

When all active sites on enzyme are involved then we will get Vmax. In Km not all active sites are engaged.

So we will get same Km but different Vmax as the concentration is different.

But to get this result there are few conditions-

  • Enzyme should possess single active site.
  • Enzyme concentration should not be too high.
Add a comment
Know the answer?
Add Answer to:
Isolation of a certain enzyme by two different scientists produce solutions of pure enzyme but with...
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
  • yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have...

    yule grapn below comparing two different enzymes with different enzyme kinetics. a. Do the graphs have any of the same values for their Vmax, Vmax/2 or Km? If so which are the affinity for substrate same which are different? Enzyme with high Enzyme with low affinity for substrate Difference in reaction rate at low [5] Reaction rater Low (S] Substrate concentration [5] b. READ THIS: Enzyme-substrate affinity is the tendency for enzyme and substrate to bind together and form the...

  • The following data has been obtained for an enzyme-catalyzed reaction with two different initial enzyme concentrations...

    The following data has been obtained for an enzyme-catalyzed reaction with two different initial enzyme concentrations of 0.025g/L and 0.015g/L. V (g/L.min) [S] (g/L) Eo = 0.025g/L Ep = 0.015g/L 56.8 1.75 1.05 28.4 1.58 0.97 19.1 1.47 0.89 14.3 1.38 0.83 11.4 1.31 0.77 9.4 1.22 0.73 8.2 1.15 0.69 7.1 1.08 0.66 (a) Using the Lineweaver-Burke plot, determine Km and Vm for Eo = 0.025g/L (b) Using the Lineweaver-Burke plot, determine Km and Vm for Ep = 0.015g/L...

  • 1.How could studying chemosynthetic organisms help scientists better understand the development of life on Earth? 2....

    1.How could studying chemosynthetic organisms help scientists better understand the development of life on Earth? 2. Why might fatty acids, amino acids and nucleic acids raise the concentration of hydrogen ions in a solution? 3. A company that makes nutritional products develops a new type of protein drink for athletes. One of the company's scientists studies the pH at which a digestive enzyme better breaks down the different proteins in the drink. The scientist uses the following experimental procedure: Five...

  • 4. Three different enzymes (A, B, C) have been found to catalyze the same reaction using...

    4. Three different enzymes (A, B, C) have been found to catalyze the same reaction using the same substrate. When you compare the three enzymes under identical conditions, you find the following: Enzyme KM (mM) 10.0 0.8 Vmax (mM/min) 450 B 100 C 3.2 0.01 A) Based on the above data, which of the enzymes will make the most product in five minutes? Assume each enzyme is saturated. Which parameter did you use to determine the order and why? B)...

  • You have an enzyme that uses two substrates in a random reaction (the order of binding...

    You have an enzyme that uses two substrates in a random reaction (the order of binding of the substrates is random). And the reaction A + B à P is catalyzed by the enzyme bringtogetherase You have carried out five sets of reaction rates Keeping B constant and varying A and then increasing B and Vary ing A again until all combinations of A and B are measured. In the reaction you used 0.02 mg of bringtogetherase which is a...

  • Question 4 Multi-Part Questions. Make sure to answer ALL parts (a-c)! You have isolated two versions...

    Question 4 Multi-Part Questions. Make sure to answer ALL parts (a-c)! You have isolated two versions of the same enzyme, a wild type and mutant. The marteses You have determined the following kinetic characteristics for each of the enzymes. Vmax Wild Type Km 200 umol / min 0.2mm Mutant 2 umol / min 20mm and the reaction is a two-step reaction where k.1 is much larger than k3, which enzyme has the higher affinity for substrate to you You determine...

  • 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...

  • You have an enzyme that uses two substrates in a random reaction (the order of binding of the substrates is random). And the reaction A + B à P is catalyzed by the enzyme bringtogetherase You have car...

    You have an enzyme that uses two substrates in a random reaction (the order of binding of the substrates is random). And the reaction A + B à P is catalyzed by the enzyme bringtogetherase You have carried out five sets of reaction rates Keeping B constant and varying A and then increasing B and Vary ing A again until all combinations of A and B are measured. In the reaction you used 0.02 mg of bringtogetherase which is a...

  • 1- Describe two attributes that are different for hemoglobin and myoglobin; focus on characteristics that are...

    1- Describe two attributes that are different for hemoglobin and myoglobin; focus on characteristics that are a direct consequence of differences in tertiary and/or quaternary structure. For each attribute, be sure to specifically explain how 3° and 4° organization impacts the described differences. 2- The kinetics of an enzyme (E)-catalyzed reaction are measured over a range of substrate (S) concentrations in the presence or absence of a reversible inhibitor (I). The total enzyme concentration is 10 uM, and the inhibitor...

  • The beaker in the illustration below contains two solutions of salt with different concentrations (measured by...

    The beaker in the illustration below contains two solutions of salt with different concentrations (measured by molarity, M). The two solutions are separated by a membrane that is permeable to both salt and water. A 0.2 M0.9MB 0.2 M salt Biology: How Life Works, Second Edition O2016 W.H. Freeman and Company Which of the following will you observe immediately in this container? Net diffusion of water across the membrane, but not of salt. Net diffusion of water from B to...

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