Problem 2:
Contrast the regulation of glycogen phosphorylase by allosteric and covalent modification mechanisms.

Regulation by allosterically

Problem 2: Contrast the regulation of glycogen phosphorylase by allosteric and covalent modification mechanisms.
Which is not involved in the regulation of glycogen phosphorylase? A) Allosteric inhibition of phosphorylase by ATP B) Indirect, positive regulation by glucagon C) Phosphorylation of phosphorylase by protein kinase A (PKA) D) Direct and indirect regulation by protein phosphatase 1 (PP1) E) Indirect, negative regulation by protein phosphatase 2B (PP2B)
Explain two mechanisms of proteins regulation. Include one mechanism that uses covalent modification (include enzymes that modify in your explanation) and one mechanism of allosteric regulation. Give specific examples of each.
Q5. The phosphorylase enzyme, which is involved in breakdown of glycogen to glucose, is controlled by both allosteric mechanisms and posttranslational modification. A) Describe how the T to R transition and activity of glycogen phosphorylase would change under the following conditions: i) high AMP levels and activation of phosphoprotein phosphatase, ii) activation of phosphorylase kinase, ili) activation of phosphorylase kinase and high glucose levels. B) What properties would an uncompetitive inhibitor of glycogen phosphorylase have, what would the Lineweaver Burk...
What differences are there between covalent and allosteric modification?
I had this partially wrong too
The muscle and liver forms of glycogen phosphorylase respond to different allosteric effectors consistent with the energy status of a given tissue. Select the correct type of regulation with the correct isozyme. AMP ATP Activates liver phosphorylase a Activates liver phosphorylase b Glucose Inhibits liver phosphorylase a Inhibits liver phosphorylase b Glucose 6-phosphate Activates muscle phosphorylase a Activates muscle phosphorylase b Inhibits muscle phosphorylase a | Inhibits muscle phosphorylase b
Describe how the opposing processes of glycogen breakdown and synthesis are reciprocally regulated by allosteric interactions and the covalent modification of key enzymes.
Regulation of the rate of an enzyme-mediated metabolic pathway can be affected by _________________. A. covalent modification of the enzyme B. allosteric modification of the enzyme C. concentration of the substrate D. A and B are correct E. A, B, and C are correct
The metabolism of fatty acids is regulated in the short term by allosteric modulators, covalent modification and _________. Group of answer choices: A) Fluctuating nutrient availability B) Energy demands C) Changes in gene expression D) Hormones E) A, B and C are all correct
Regulation a) Please list two types of reversible covalent modification of proteins used for regulation b) How is chymotrypsin activated in the digestive system? c) Why is phosphorylation an effective means of regulating protein activity? d) What is the cascade for zymogen activation in the digestive system? e) What posttranslational modification does prothrombin undergo before it is converted to thrombin 1) What is the function of vitamin K?
A pharmaceutical research group is studying the allosteric regulation mechanisms for an enzyme involved in kidney cancer. They perform a number of different assays and make the following observations. Using these observations, determine whether the model is most consistent with a. induced-fit/sequential b. MWC/symmetry c. both models Observations: -the enzyme's allostertic activator binds to an allosteric site located 1.5 nanometers away from the active site. -when the allosteric activator binds to the allosteric site, NMR signals indicate that a significiant...