Role of Cofactors and Prosthetic Groups in Conjugated Enzymes

Conjugated enzyme

an enzyme that has a nonprotein part in addition to a protein part

A conjugated enzyme, also known as a holoenzyme, is a catalytically active protein molecule consisting of an apoenzyme and a cofactor or prosthetic group. The apoenzyme is the protein part of the enzyme, which alone is not catalytically active and requires a cofactor or prosthetic group to form a complete, active holoenzyme.

Cofactors and prosthetic groups are non-protein molecules that can bind to and activate an apoenzyme, allowing it to carry out a specific chemical reaction. Cofactors can be small organic molecules, such as vitamins or metal ions, while prosthetic groups are typically larger and more complex molecules, such as heme or flavin.

Once the cofactor or prosthetic group binds to the apoenzyme, the active site of the enzyme is formed, which is where the catalytic reaction takes place. The conjugated enzyme can then catalyze a specific chemical reaction, such as breaking down a substrate or building up a product.

Overall, the presence of a cofactor or prosthetic group can greatly increase the activity and specificity of an enzyme, allowing it to carry out its function more efficiently.

More Answers:

Crucial Role of Active Site in Enzyme Catalysis
Unlocking the Power of Cofactors and Prosthetic Groups in Holoenzymes: A Comprehensive Explanation
Apoenzymes and Their Role in Enzyme Activity: Importance of Cofactors and Coenzymes.

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