4. Enzyme performance (a) Compare chymotrypsin, MutY, and carbonic anhydrase interms of chemical difficulty. (Hint: compare kcat). (b) Which enzyme is faster? And byhow much? (c) Draw a molecular sketch comparing TS stabilization strategies for Mutyand chymotrypsin. (d) Compare chymotrypsin, Muty, and carbonic anhydrase in termsof how quickly they find their substrates. (Hint: compare kcat/KM). Which enzyme hasthe more "perfect" enzyme performance rating? (e) What is the molecular explanation forthe apparently impossible fast rate at which Muty finds its substrate? (f) What is thebiological constraint demanding this very high level of enzyme performance?Enzyme\ParameterCarbonic anhydraseMutyChymotrypsinkcat (s-1)600,0000.2100KM (M)0.0081.2 x 10-100.005

Turnover number (kcat) is the maximum number of substrate molecules that can be converted into…

Answered: Enzyme performance (a) Compare…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter25: Nitrogen Acquisition And Amino Acid Metabolism

Section: Chapter Questions

Problem 21P

See similar textbooks

Similar questions

Which reaction is catalyzed by carbonic anhydrase? a. HPO42+H+H2PO4 b. CO2+H2OH2CO3 c. H2PO4+OHPHO42+H2O d. H2CO3HCO3+H+
Do you think that the Ea for ATP hydrolysis is relatively low or high? Explain your reasoning.
Describe the position of the transition state on a vertical energy scale, from low to high, relative to the position of the reactants and products, for both endergonic and exergonic reactions.
MATHEMATICAL The kinetic data in the following table were obtained for the reaction of carbon dioxide and water to produce bicarbonate and hydrogen ion catalyzed by carbonic anhydrase: CO2+H2OHCO3+H+ [H. De Voe and G. B. Kistiakowsky, J. Am. Chem. Soc. 83, 274 (1961)]. From these data, determine KM and Vmax for the reaction. CarbonDioxideconcentration(mmolL1)1/Velocity(M1sec)1.252.55.020.00.25036103201031210361030.256
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
What is the primary difference between a circular pathway and a linear pathway?
MATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?
MATHEMATICAL The hydrolysis of a phenylalanine-containing peptide is catalyzed by -chymotrypsin with the following results. Calculate KM and Vmax for the reaction. PeptideConcentration(M)Velocity(Mmin1)2.51045.010410.010415.01042.21065.81065.91067.1106
Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.
The energy released by the hydrolysis of ATP is primarily stored between the alpha and beta phosphates equal to -57 kcal/mol harnessed as heat energy by the cell to perform work providing energy to coupled reactions
Understanding the Action of Fluoroacetate on the TCA Cycle In a tissue where the TCA cycle has been inhibited by fluoroacetate, what difference in the concentration of each TCA cycle metabolite would you expect, compared with a normal, uninhibited tissue?
With regard to enzymes, why are vitamins necessary for good health? Give examples.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology: The Dynamic Science (MindTap Course List)

Biology

ISBN:

9781305389892

Author:

Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:

Cengage Learning

Anatomy & Physiology

Biology

ISBN:

9781938168130

Author:

Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble

Publisher:

OpenStax College

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology: The Dynamic Science (MindTap Course List)

Biology

ISBN:

9781305389892

Author:

Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:

Cengage Learning

Anatomy & Physiology

Biology

ISBN:

9781938168130

Author:

Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble

Publisher:

OpenStax College

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Curren'S Math For Meds: Dosages & Sol

Nursing

ISBN:

9781305143531

Author:

CURREN

Publisher:

Cengage

Biochemistry

ISBN:

9781305961135

Author:

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

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS