(Integrates with Chapter 24 .) Acetyl-CoA carboxylase has at least seven possible phosphorylation sites (residues 23,25,29,76,77 \(95,\) and 1200 ) in its 2345 -residue polypeptide (see Figure 24.4 ). How many different covalently modified forms of acetyl-CoA carboxylase protein are possible if there are seven phosphorylation sites?

Short Answer

Expert verified
There are \(2^7=128\) different covalently modified forms of acetyl-CoA carboxylase possible assuming there are seven phosphorylation sites.

Step by step solution

01

Understanding the Scenario

Acetyl-CoA carboxylase, in this case, can be phosphorylated at 7 different positions. Each of these positions can either be phosphorylated or not, generating 2 possible states at each site.
02

Calculate the Possible Modifications

As each site can exist in two different states, and there are 7 such independent sites, the total number of possible modifications can be calculated using the formula of permutations for binary systems, which is \(2^n\), where n is the number of sites. In this case, n=7.
03

Compute the Result

Substitute n=7 in the equation \(2^n\) to calculate the result, which will give the total number possible covalently modified forms of Acetyl-CoA carboxylase.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Protein Phosphorylation
Protein phosphorylation is a vital cellular process that plays a significant role in the regulation of various functions within a cell. It involves the addition of a phosphate group, typically derived from adenosine triphosphate (ATP), to one or several amino acids in a protein molecule. This phosphorylation event is catalyzed by enzymes known as kinases.

The impact of phosphorylation on a protein can range from changes in its enzymatic activity, alterations in its interaction with other proteins, to the modification of its stability. For example, in the exercise, Acetyl-CoA carboxylase can be phosphorylated at seven distinct sites. This phosphorylation is a form of regulation of the enzyme, which can lead to changes in its activity. Introducing a phosphate group into the protein typically results in a conformational change, which can either inhibit or activate the enzyme's function.
Enzyme Modification
Enzyme modification is an intricate part of cellular regulation, wherein the activity, stability, or function of an enzyme can be altered through various biochemical modifications. One common form of enzyme modification is phosphorylation, which is highly relevant to the exercise at hand involving Acetyl-CoA carboxylase. However, enzymes can also be modified in other ways, such as acetylation, methylation, ubiquitination, and more.

These modifications can act as molecular switches that turn enzyme activity on or off or modulate it to fine-tune the cell's metabolic processes. In our example, the modification via phosphorylation at different sites can create a diversity of enzyme states, potentially leading to a complex regulation mechanism. This enables the cell to respond dynamically to different metabolic needs or environmental cues.
Post-Translational Modifications
Post-translational modifications (PTMs) refer to the chemical alterations that proteins undergo after their synthesis in the ribosome. Phosphorylation, as seen with Acetyl-CoA carboxylase, is just one type of PTM. These modifications extend the range of functions of the protein by introducing new functional groups, changing its structure, location or interactions, and even marking it for degradation.

PTMs are essential for the complexity and diversity of the proteome. With seven potential phosphorylation sites, Acetyl-CoA carboxylase illustrates how PTMs provide a vast array of possibilities for enzyme regulation. Each PTM can affect the protein's function in a unique way. So, expanding on our exercise, with seven potential sites for PTM and two possible states per site (phosphorylated or not), there can be a maximum of \(2^7\) or 128 possible modified forms of Acetyl-CoA carboxylase, each potentially having a different role in the cell.

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