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Chapter 15: Problem 12

What are the relative advantages (and disadvantages) of allosteric regulation versus covalent modification?

Short Answer

Expert verified
Allosteric regulation, while quick and reversible in action, may pose limitations for long-term control of processes due to its rapid reversibility. Covalent modification, on the other hand, while apt for long-term regulation, may demand additional energy and enzymes for reversal, posing a limitation for processes that need quick starting and stopping.

Step by step solution

01

Understanding Allosteric Regulation

Allosteric regulation involves the binding of a regulatory molecule at a location other than the active site (known as the allosteric site) which causes a conformational change in the protein structure, affecting its function. This is a non-covalent, reversible interaction.
02

Advantages and Disadvantages of Allosteric Regulation

The main advantage of allosteric regulation is its reversibility and rapid response. Allosteric enzymes can quickly switch between their active and inactive states without the need for additional enzymes. This is beneficial for controlling processes within the cell in a timely manner. The disadvantage, however, may be that this rapid response may not be suitable for longer-term regulation of cellular processes.
03

Understanding Covalent Modification

Covalent modification regulates enzyme activity by adding or removing chemical groups (like phosphate, methyl etc.) through covalent bonding. This is often an irreversible process and involves enzyme catalyst. The protein structure and function can significantly change as a result of this modification.
04

Advantages and Disadvantages of Covalent Modification.

The main advantage of covalent modification is its lasting effect. This method of regulation is best suited for long-term regulation of cellular processes. On the downside, the changes are often irreversible, and reversing the modification, when required, would demand additional energy and enzymes.

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Most popular questions from this chapter

(Integrates with Chapter \(13 .\) ) Draw both Lineweaver-Burk plots and Hanes- Woolf plots for an MWC allosteric enzyme system, showing separate curves for the kinetic response in (a) the absence of any effectors, (b) the presence of allosteric activator \(A,\) and \((c)\) the presence of allosteric inhibitor I.

Figure 15.17 traces the activation of glycogen phosphorylase from hormone to phosphorylation of the \(b\) form of glycogen phosphorylase to the \(a\) form. These effects are reversible when hormone disappears. Suggest reactions by which such reversibility is achieved.

If no precautions are taken, blood that has been stored for some time becomes depleted in \(2,3-\mathrm{BPG}\). What happens if such blood is used in a transfusion?

You land a post as scientific investigator with a pharmaceutical company that would like to develop drugs to treat people with sickle-cell anemia. They want ideas from you! What molecular properties of Hb S might you suggest as potential targets of drug therapy?

Why do you suppose proteolytic enzymes are often synthesized as inactive zymogens?
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