i submitted this 3 times in bartleby and everyone gave differnt answers please answer correctly Which of the following statements about enzyme regulation is incorrect?Feedback inhibition is a mode of enzyme regulation employing negative allostery, where thefinal product of a pathway inhibits the first step of the same pathwayThe differential KM and Vmax of hexokinase isoforms between the liver and muscle allows thetuning of enzyme activity to different substrate concentrations and overall tissue functionThe covalent modification of enzymes is a mechanism of regulation requiring kinase activity toinstall the phosphate, but where dephosphorylation can't occur spontaneouslyProteolytic activation of enzymes converts a zymogen to an active enzyme by removal ofpeptide components and/or rearrangement of the protein backbone.All answers are correct

Enzyme regulation is either increasing or decreasing the enzyme's activity by using a effector…

Answered: Which of the following statements about…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter17: Metabolism: An Overview

Section: Chapter Questions

Problem 15P

See similar textbooks

Similar questions

Which of the following is likely to be correct if all mutases are completely inhibited?a. Removal of glucosyl residues from nonreducing ends of glycogen in the liver is compromised;therefore, release of free glucose into blood from the liver would decreaseb. Glycerol can be efficiently converted into glucose but cannot be efficiently converted into glucosylresidues in glycogen in the liverc. Bothaandbd. Neither a nor b
Many biosynthetic pathways are regulated by feedback control, where the product of a pathway turns off an enzyme that catalyzes an early step in the pathway. Usually, this control comes from an allosteric interaction. Of the types of reversible enzyme inhibition (Competitive inhibition, Noncompetitive inhibition, and Uncompetitive inhibition), what type is most likely to occur in a feedback control mechanism like this and why?
The effectiveness of allosteric effectors in regulating metabolic pathways is based on their ability to— interact with multiple substrate-binding sites on the target enzyme(s). interfere with competitive inhibitors. alter the concentration of the target enzyme(s). denature the target enzyme(s). change the conformation of the target enzyme(s).
The binding of insulin to its receptor on the surface of atarget cell activates the receptor’s tyrosine kinase activity,which in turn causes several phosphorylation cascades thatalter the activity of numerous enzymes and alters the expression of genes. Describe how one of these phosphorylationcascades stimulates glycogen synthesis.
Which of the following statements about allosteric enzyme regulations are true. A. Allosteric regulations is always used to negatively regulate enzyme activity. B. Allosteric regulations are often end products of a biochemical pathway. C. Diffrent allosteric regulators turn enzyme activity on or off by binding the same site. D. Binding of allosteric regulators alters the conformation of an enzyme. B only B and C B and D D only A and D
The synthesis of enzymes in response to changing metabolicneeds is referred to as _____________________.
iodoacetate is an irreversible inhibitor of glyceraldehyde-3-phosphate dehydrogenase. which of the following is the expected outcome of the exposure of a cell to iodoacetate - Cellular resiration will stop if the cell solely depends on glucose as fuel - The rate of cellular respiration will increase - The reoxidation of coenzymes will noy be affected , but the efficiency of oxidative phosphorylation will be diminished - There will be no effect on cellular respiration as long as the cell has a large glucose reserve -The cell sill not be able to reoxidize the reduced coenzymes
What will happen to the rate of FPP synthesis when FPP concentration is very high Inhibition of an enzyme by its product (or a downstream product of the same pathway) is a common mechanism of enzyme regulation. Explain the utility of this mechanism
The active (catalytic) site of an enzyme contains the side chains of amino acid residues that areconserved because they participate in the protein’s catalytic activity. The bulk of the enzyme,however, is not part of the active site. A substantial amount of energy is required to synthesizeenzymes. Why are these molecules so large?
enzyme e helps to catalyse the conversion of substrate s to product p which of the following parameters would change in response to increasing the concentration of E in this reaction - both the vmax and catalytic efficiency of enzyme e - the catalytic efficiency of enzyme e - both catalytic efficiency for E and affinity of enzyme e for substrate S - turnover number of enzymes - affinity of enzyme E for substrate S
Assume that an inhibitor (I) can bind to an enzyme and is modified by the enzyme. The modified inhibitor (I*) is then permanently associated with the active site of the enzyme, thus inhibiting the enzyme activity. Such inhibitors are called: Suicide substrates Transition-state analogs Both A and B Neither A nor Bwhich answer choice is correct im confused... thx
Several of the enzymes of glycolysis fall into classes that we will see often in metabolism. What reaction types are catalyzed by each of the following: (a) Kinases (b) Isomerases (c) Aldolases (d) Dehydrogenases

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology (MindTap Course List)

Biology

ISBN:

9781337392938

Author:

Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology (MindTap Course List)

Biology

ISBN:

9781337392938

Author:

Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS