ou have been researching two additional methyltransferase enzymes that catalyze the same reaction.  At a concentration of 10 nMoles enzyme, Enzyme A has a Km of 60 mmol, while Enzyme B has a Km of 2 mmol for the reaction conditions. You have two solutions (A and B) with equal amounts of Enzyme A in tube A and Enzyme B in tube B respectively. They both have the same Vmax of 500 mmol/second. Which enzyme would have a higher reaction velocity with the substrate concentration of 30 mmol?  Why?  Give approximate reaction velocity values for each enzyme (mmol/s)  Would this result change if the substrate was 1000 and 1,000,000 mmol? Explain why, and give approximate reaction velocity concentrations.   An irreversible inhibitor has been added to the reaction mixes A and B.  It binds with 100% affinity for Enzyme A, but does not bind to Enzyme B.  If 5 nMoles of inhibitor is added to the reaction, what would happen to the apparent Km and Vmax of Enzyme A and B?

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
icon
Related questions
icon
Concept explainers
Question

You have been researching two additional methyltransferase enzymes that catalyze the same reaction.  At a concentration of 10 nMoles enzyme, Enzyme A has a Km of 60 mmol, while Enzyme B has a Km of 2 mmol for the reaction conditions. You have two solutions (A and B) with equal amounts of Enzyme A in tube A and Enzyme B in tube B respectively. They both have the same Vmax of 500 mmol/second.

  1. Which enzyme would have a higher reaction velocity with the substrate concentration of 30 mmol?  Why?  Give approximate reaction velocity values for each enzyme (mmol/s) 
  2. Would this result change if the substrate was 1000 and 1,000,000 mmol? Explain why, and give approximate reaction velocity concentrations.  
  3. An irreversible inhibitor has been added to the reaction mixes A and B.  It binds with 100% affinity for Enzyme A, but does not bind to Enzyme B.  If 5 nMoles of inhibitor is added to the reaction, what would happen to the apparent Km and Vmax of Enzyme A and B?
Expert Solution
steps

Step by step

Solved in 5 steps with 8 images

Blurred answer
Knowledge Booster
Molecular techniques
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.
Similar questions
  • SEE MORE QUESTIONS
Recommended textbooks for you
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON