What are the advantages to regulating enzyme activity through
phosphorylation?
How does it differ from allosteric regulation and how is it
similar?
Are there any advantages to phosphorylation versus allosteric
regulation of protein function?
The advantange to regulating enzyme activity through phosphorylation is that: In phosphorylation the enzyme used for catalysing reaction is protein kinase which constitute one of the largest protein families known, with more than 100 homologous enzyme in yeast and more than 550 in human beings. This multiplicity of emzymesallows regulation to be fine tuned according to a specific tissue, time, or substrate.
In allosteric regulation, the regulatory molecule is not covalently attached attached to the protein while phosphorylation is the covalent addition of the phosphate group to apecific amino acid side chains.
What are the advantages to regulating enzyme activity through phosphorylation? How does it differ from allosteric...
How you would determine an enzyme regulation? Below is a series of results from tests of one particular enzyme. List all the potential methods of regulation still possible after each test. The options are: "genetic" control, zymogenic, phosphorylation, competitive inhibition, noncompetitive inhibition, positive allosteric regulation, and irreversible inhibition. 1. The enzyme is always present in the cell. 2. All tests only slow enzyme activity. 3. Adding more substrate does not increase reaction rate. 4. There seems to be a form...
How does the binding of a regulatory molecule to the allosteric site affect the activity of an enzyme? Group of answer choices A. It may decrease the activity of the enzyme. B. It may change the shape of the substrate. C. It may change the affinity of the enzyme for its substrate. All of the above A and C
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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?
Correct answer and why the other ones are wrong 3. How does phosphorylation regulate protein activity? a. It adds energy to the protein b. The negative charge associated with the phosphate group blocks the binding of negatively charged molecules c. It causes a conformational change in the protein d. It denatures the protein.
ATCase is an important enzyme in DNA replication. a) What does this enzyme do and what are its substrates? b) This enzyme demonstrates feedback regulation. Describe its quaternary structure in this regard. c) Besides substrate(s) and product, what other molecules are involved in the feedback regulation of ATCase? Describe their function and how they interact?
ATCase is an important enzyme in DNA replication. a) What does this enzyme do and what are its substrates? b) This enzyme demonstrates feedback regulation. Describe its quaternary structure in this regard. c) Besides substrate(s) and product, what other molecules are involved in the feedback regulation of ATCase? Describe their function and how they interact?
Can any one do 2 and 3 Pyruvate kinase is one of the irreversible steps of glycolysis. The human genome has four genes that encode different pyruvate kinases, including a muscle specific form and a liver specific form. The liver specific form differs from the muscle specific form since it has additional regulation through phosphorylation by protein kinase A and allosteric regulation by the amino acid alanine. A V. vs. [S] plot of liver pyruvate kinase is shown below. hi...
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