Metabolic flux is regulated by both availability of substrates and level ofenzyme activity. Match the mechanism by which enzyme activity is regulated(A, B, C) with a specific example of this type of regulation (1, 2, 3, 4, 5, 6).Each mechanism is associated with two specific examples.Mechanism of RegulationA. Catalytic activityB. CompartmentationC. Enzyme levelsA:1,5; B:3,4; C:2,6OA:1,5; B:3,6; C:2,4A:2,5: B:3.4. C.16Example ofRegulation1. covalentmodification4. subcellularlocalization2. protein synthesis 5. allosteric control3. tissuelocalization6. gene transcription

Enzymes are proteins which increase the rate of biochemical reactions. They carry out the quick…

Answered: Metabolic flux is regulated by both…

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

please answer
In drug development, enzyme inhibition studies play a very important role since drugs are often used to target specific enzymes, as illustrated in the example of lovastatin. An important consideration when assessing drug potential is the drug's affinity for the selected target. (The higher the affinity, the better the candidate.) The K₁ is often used in studies to measure the affinity of drug candidates toward their target. Based on your understanding of K₁, which drug would be the BEST candidate for further development? Drug C: K₁= 9.1 x 107 M Drug E: K₁ = 3.5 × 10³ mm Drug D: K₁=5.5 × 10³ μM Drug B: K₁=2.5 × 10 mm Drug A: K₁=4.5 x 10 mm
A newly developed drug is suspected to act by inhibiting its enzymatic target. To test this, the rates of reaction in the presence and absence of the new drug were determined. The results of these experiments have been plotted as a double reciprocal plot shown in figure 1 below. Using this figure, calculate the values of Vmax and Km for the enzyme in the presence and absence of the drug. 2. Based on the figure and your answer, what type of inhibition is the new drug displaying? 3. Briefly explain how this type of inhibition exerts its action on an enzyme. Figure 1: Double reciprocal plot of reaction rate against substrate concentration in the presence and absence of a new drug.
Which of the following is incorrect about the enzyme chymotrypsin? a. It catalyzes the addition of water across a double bond O b. It is known as a serine protease O c. Artificial substrates are used to monitor the reaction catalyzed by the enzyme d. It is classified as a hydrolase
How do non-competitive inhibitors affect KM and Vmax? (explain with details) Feedback inhibition typically impedes the activity of the enzyme that catalyzes the first committed step of a metabolic pathway, rather than an enzyme that catalyzes a later step in the pathway. Why is this adaptive?
Which of the following statements about enzyme regulation is NOT true? a. covalent modification is one type of enzyme regulation. b. biologically most important type of regulation is standard inhibition. c. allosteric regulation can involved feedback inhibition. d. some types of enzume regulation are not widely used in biology. e. none of the above
Select all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.
It makes sense that enzymes should be active when they are needed and inactive when they are not needed. Non-competitive (allosteric) regulation of enzymes is important in metabolism because it allows for the rapid adjustment of their activity. Recall hexokinase, a key enzyme of glycolysis. Which of the following molecules likely functions as an allosteric inhibitor of its activity? A. ADP B. Glucose C. NAD+ D. Pyruvate
b. You conduct some additional experiments to elucidate the starlase metabolic pathway. Your results are shown below. Use this information alongside information from the complementation table above to place the intermediates in the correct order on the pathway. (HINT: use the complementation groups from the table above to help you consolidate information on the tables below. Reference practice question 3 from today's lecture for help). Mutant 1 2 3 4 5 6 Precursor --> [Select] None [Select] Addition to minimal medium starlase + + + + + + --> starlase P + + [Select ] T + O + c. Mutant 2 has a loss-of-function mutation for which enzyme in the starlase synthesis pathway? [Select] E1 E2 E3 E4 Precursor → Intermediate 1 → Intermediate 2 → Intermediate 3 → starlase
Which type of potato do you think would be the best source of obtaining tyrosinase; a normal white potato or a sweet potato? Consider all the factors that might go into this decision (total amount of the enzyme, the enzyme activity and its specific activity). Give a brief description of your reasoning.

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