Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 6, Problem 65TQ
Summary Introduction
To review:
The Km and Vmax for the uninhibited enzyme is to be determined.
Introduction:
The enzymes are the protein molecules with catalytic properties. The enzyme enhances the rate of the reaction without altering the equilibrium. The substrates are the molecules on which an enzyme act and product is formed on conversion of the substrate.
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What kind of inhibitor is threo-sphingosine? Explain this type of inhibition.
Can you please help me answer the following question in three paragraphs and in your own words.
1. How do you determine the effects of substrate concentration on enzyme activity? (Do not write a procedure just give as many details as possible. Please make sure this is at least in three paragraphs and in your own words).
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3.
CO2 + H20 > H+ + HCO3
There are many different isoforms of this enzyme. (see for instance
http://en.wikipedia.org/wiki/Carbonic_anhydrase
1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
Chapter 6 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 6 - Prob. 1QCh. 6 - Prob. 2QCh. 6 - Prob. 3QCh. 6 - Prob. 4QCh. 6 - Prob. 5QCh. 6 - Prob. 6QCh. 6 - Prob. 7QCh. 6 - Prob. 8QCh. 6 - Prob. 9QCh. 6 - Prob. 1RQ
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- The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…arrow_forwardThis is a conjectural question: If the reactive part of coenzyme A is the thioester, why is the molecule socomplicated?arrow_forwardAll coenzymes are cofactors, but not all cofactors are coenzymes. Explain this statement briefly.arrow_forward
- What are catalases? Why are they called antioxidant enzymes? Give the industrial applications of this enzyme.arrow_forwardThe following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.arrow_forwardEnzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of substrate intoproduct. Why is such specificity inherent in theirstructure?arrow_forward
- Why are such allosteric enzymes composed of more than one catalytic subunit?arrow_forwardGive the two reasons why anabolic reactions in metabolism are not exactly the reverse of catabolic pathway.arrow_forwardWhat is the simplest explanation in the notion that phosphofructokinase is a regulated enzyme?arrow_forward
- Given this reaction productarrow_forwardHexokinase is an example of a general class of enzymeknown as the _____________________.arrow_forwardThe uncatalyzed reaction rate for the conversion of substrate X to product Y is one year. The enzyme-catalyzedrate is one millisecond. Describe the features of theenzyme that are probably responsible for this ratedifference.arrow_forward
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