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Introduction:
Non-peptide (non-protein) molecules called prosthetic groups to bind to proteins and help them in various ways. They might be inorganic (metals) or organic (carbon-based) and have a strong affinity for their target. Covalent (electron-sharing) or non-covalent bonds can be used to bind prosthetic groups.
In cellular function, what role does it play?
Prosthetic groups are required for electron transport in cellular/mitochondrial respiration, which is where the cell produces ATP (adenosine triphosphate), the energy that cells require to function and keep you alive. They also play a role in photosynthesis, which is a vital activity for plants to survive. Furthermore, prosthetic groups have a role in the synthesis of fatty acids, which are essential for a range of cellular functions, including respiration.
Functions:
Prosthetic groups, like prosthetic limbs, can assist patients to do a range of actions like walking, running, chopping onions, and picking up their shoes. They mostly help proteins, but they aren’t limited to that. Prosthetic groups can help proteins fold into a 3-D shape by acting as scaffolding or a tie (their conformation).
They can also assist a cell in transporting electrons or molecules from one location to another by assisting proteins in binding other cellular components or acting as transporters of electrons or molecules (protons (H+) and oxygen). Prosthetic groups can activate enzymes (turn them on) or improve their activity by binding to a certain set of proteins known as enzymes.
Cofactors or coenzymes are prosthetic groups that connect to enzymes and aid in their action. A holoenzyme is a protein that has a prosthetic group, while a holoprotein is any protein that has a prosthetic group.
Examples:
Non-protein components known as prosthetic groups bind to proteins and help them in a variety of ways. Holoproteins are prosthetic groups that are bound to proteins. Heme, biotin, flavin, iron sulphides, copper, and ubiquinone are examples of prosthetic groups.
Comparison of Prosthetic Groups and Coenzymes:
Prosthetic Groups | Coenzymes |
By interacting with the apoenzyme, it aids the enzyme’s action. | Facilitates the enzyme’s biological transition. |
The enzyme is tightly coupled or stably connected with it. | The enzyme is loosely linked to it. |
Metal ions or tiny organic molecules are the two types of ions. | Organic molecules of a small size. |
Examples: Organic molecules like biotin, heme, and metal ions like Mg, Fe, and Cu | Examples: Vitamin B12, Coenzyme A |
Comparison of Prosthetic Groups and CoFactor:
Prosthetic Group | Cofactor |
With the protein portion, it forms a covalent or permanent link. | It creates a covalent connection with a non-protein component here. |
These are organic substances. | This is a list of inorganic chemicals. |
These substances serve as transporters. | The reaction speed is accelerated by these substances. |
This is the chemical molecule in the protein that transports chemicals to the enzymes. | The enzyme is bound by a non-protein chemical. |
Organic compounds such as vitamins and vital minerals are examples. | Metal ions such as potassium and zinc are examples. |
Conclusion:
Cofactors that bind strongly to proteins or enzymes are known as prosthetic groups.
They might be organic or metal ions and they are frequently covalently bound to proteins. Cofactors can connect to a variety of enzymes, and they can attach to some enzymes loosely as a coenzyme and others tightly as a prosthetic group. Some cofactors may always bind to their enzymes tightly.
Other proteins besides enzymes can bind to the prosthetic groups.
