An enzyme catalyzes the reaction A --> B. The enzyme is present at aconcentration of 2 nM, and the Vmax is 10 uM/s. The Km for substrate A is10mMAt what substrate concentration would this enzymatic reaction be operating atonly 20 percent of its maximum rate?

The Michaelis-Menten equation can be used to relate the substrate concentration to the reaction rate…

Answered: At what substrate concentration would…

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

See similar textbooks

Similar questions

Explain the advantage of the enzymatic activity ?
Sketch a graph showing how the concentration of product P varies with time for chymotrypsin-catalysed hydrolysis using a substrate that displays both Michaelis-Menten kinetics and burst kinetics. On the same graph show the effect of doubling the enzyme concentration, keeping all other conditions the same.
What is the need of adding DNS solution to the enzyme substrate solution? What is the problem in determining rates at low substrate concentration?
What is the difference between substrate-level phosphorylation and oxidative phosphorylation? Please give an example of each.
Why do the cytochrome electron-transfer processes have different standard reduction potentials, despite the fact that they all utilize the identical iron oxidation–reduction reaction?
One of the hallmarks of competitive inhibition is that there is constant competition betweenthe substrate and the inhibitor for binding to the enzyme active site.a) If [inhibitor] >> [substrate], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?b) If [substrate] >> [inhibitor], which compound “wins” (i.e., occupies the active site a greaterpercentage of the time)?
In the pathway for degradation of BCAAs, which reaction takes place prior to the action of the BCKDC and what is the essential coenzyme for the reaction?
Describe the rate of enzyme-catalyzed reaction with increasing substrate concentration at constant enzyme concentration. In what ways does hydrogen ion concentration affect enzyme activity?
Which reversible inhibitors do not affect the substrate binding but the catalytic function of the enzyme? Why?
The enzymatic activity of an enzyme with Kg = 2 mM that converts substrate S into product P is measured at an initial substrate concentration S, of 10 µM. After 5 min, the substrate concentration is halved. What is the rate constant k, the maximal velocity vmax and the concentration of product after 12 min?
Which two enzyme curves would be generated from a themophilic bacteria that lives in a strongly acid environment? Please provide a supportive statement about why you picked each of the two curves you picked. Your answer should include information from the graphs. (a) 3 5 MA A 100 7 8 20 2 40 60 Temperature (°C) I 80 ➤ (b) 1 2 3 4 PH 5 6 ➤ 9 10
a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzyme

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

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…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

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…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS

At what substrate concentration would this enzymatic reaction be operating at only 20 percent of its maximum rate?