An enzyme called carbonic anhydrase, a monomeric protein (30,000 Daltons), catalyzes the following reaction for the hydration of CO2: H₂O + CO₂ H₂CO3 Carbon dioxide is produced in tissue as one of the final products of respiration. It then diffuses into the blood system, where it is converted to the hydrogen carbonate ion by carbonic anhydrase. The reverse reactions occur in the lungs, where CO₂(g) is expelled. We define keat as the turnover number - the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by: kcat = Vmax [E] a. Determine the value of the turnover number of the enzyme carbonic anhydrase (carbonic anhydrase has a single active site), given the following two scenarios: i. Vmax for carbonic anhydrase = 561 umol·Ls and [E] =1.40 nmol.L¹. ii. 75 ng of pure carbonic anhydrase (under saturating conditions of CO₂) catalyzes the hydration of 12 mM of CO₂ in 2min at 37°C in a 10mL solution. b. Describe in words the meaning of the keat value calculated.
An enzyme called carbonic anhydrase, a monomeric protein (30,000 Daltons), catalyzes the following reaction for the hydration of CO2: H₂O + CO₂ H₂CO3 Carbon dioxide is produced in tissue as one of the final products of respiration. It then diffuses into the blood system, where it is converted to the hydrogen carbonate ion by carbonic anhydrase. The reverse reactions occur in the lungs, where CO₂(g) is expelled. We define keat as the turnover number - the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by: kcat = Vmax [E] a. Determine the value of the turnover number of the enzyme carbonic anhydrase (carbonic anhydrase has a single active site), given the following two scenarios: i. Vmax for carbonic anhydrase = 561 umol·Ls and [E] =1.40 nmol.L¹. ii. 75 ng of pure carbonic anhydrase (under saturating conditions of CO₂) catalyzes the hydration of 12 mM of CO₂ in 2min at 37°C in a 10mL solution. b. Describe in words the meaning of the keat value calculated.
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
Related questions
Question
![An enzyme called carbonic anhydrase, a monomeric protein (30,000 Daltons), catalyzes the following reaction for
the hydration of CO2:
H₂O +
CO₂
H₂CO3
Carbon dioxide is produced in tissue as one of the final products of respiration. It then diffuses into the blood
system, where it is converted to the hydrogen carbonate ion by carbonic anhydrase. The reverse reactions occur in
the lungs, where CO₂(g) is expelled.
We define keat as the turnover number - the maximum number of substrate molecules that can be converted into
product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily
equal to the concentration of enzyme molecules because some enzyme molecules have more than one active site. If
the enzyme molecule has one active site, the turnover number is given by:
kcat =
Vmax
[E]
a. Determine the value of the turnover number of the enzyme carbonic anhydrase (carbonic anhydrase has a
single active site), given the following two scenarios:
i. Vmax for carbonic anhydrase = 561 umol·Ls and [E] =1.40 nmol.L¹.
ii. 75 ng of pure carbonic anhydrase (under saturating conditions of CO₂) catalyzes the hydration of 12 mM of
CO₂ in 2min at 37°C in a 10mL solution.
b. Describe in words the meaning of the keat value calculated.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F0ec2b5c7-78aa-4056-b0d5-acb9e9a6b1d6%2F3fa2fc8a-8bf7-45dd-ab33-d07bdc539fdd%2Fhgom4x9_processed.jpeg&w=3840&q=75)
Transcribed Image Text:An enzyme called carbonic anhydrase, a monomeric protein (30,000 Daltons), catalyzes the following reaction for
the hydration of CO2:
H₂O +
CO₂
H₂CO3
Carbon dioxide is produced in tissue as one of the final products of respiration. It then diffuses into the blood
system, where it is converted to the hydrogen carbonate ion by carbonic anhydrase. The reverse reactions occur in
the lungs, where CO₂(g) is expelled.
We define keat as the turnover number - the maximum number of substrate molecules that can be converted into
product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily
equal to the concentration of enzyme molecules because some enzyme molecules have more than one active site. If
the enzyme molecule has one active site, the turnover number is given by:
kcat =
Vmax
[E]
a. Determine the value of the turnover number of the enzyme carbonic anhydrase (carbonic anhydrase has a
single active site), given the following two scenarios:
i. Vmax for carbonic anhydrase = 561 umol·Ls and [E] =1.40 nmol.L¹.
ii. 75 ng of pure carbonic anhydrase (under saturating conditions of CO₂) catalyzes the hydration of 12 mM of
CO₂ in 2min at 37°C in a 10mL solution.
b. Describe in words the meaning of the keat value calculated.
AI-Generated Solution
Unlock instant AI solutions
Tap the button
to generate a solution
Recommended textbooks for you

Chemistry
Chemistry
ISBN:
9781305957404
Author:
Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781259911156
Author:
Raymond Chang Dr., Jason Overby Professor
Publisher:
McGraw-Hill Education

Principles of Instrumental Analysis
Chemistry
ISBN:
9781305577213
Author:
Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781305957404
Author:
Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:
Cengage Learning

Chemistry
Chemistry
ISBN:
9781259911156
Author:
Raymond Chang Dr., Jason Overby Professor
Publisher:
McGraw-Hill Education

Principles of Instrumental Analysis
Chemistry
ISBN:
9781305577213
Author:
Douglas A. Skoog, F. James Holler, Stanley R. Crouch
Publisher:
Cengage Learning

Organic Chemistry
Chemistry
ISBN:
9780078021558
Author:
Janice Gorzynski Smith Dr.
Publisher:
McGraw-Hill Education

Chemistry: Principles and Reactions
Chemistry
ISBN:
9781305079373
Author:
William L. Masterton, Cecile N. Hurley
Publisher:
Cengage Learning

Elementary Principles of Chemical Processes, Bind…
Chemistry
ISBN:
9781118431221
Author:
Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:
WILEY