Final answer:
A conjugated enzyme consists of an apoenzyme and a non-protein cofactor forming a holoenzyme. The enzyme's active site is where the substrate binds, facilitated by a specific and complementary shape/configuration of amino acids, enabling the formation of an enzyme-substrate complex leading to the catalytic reaction.
Step-by-step explanation:
Components of a Conjugated Enzyme
The components of a conjugated enzyme include the protein portion, known as the apoenzyme, and a non-protein component referred to as the cofactor.
When these two components come together, they form a holoenzyme, which is the active conjugated enzyme.
The protein portion alone is inactive without this non-protein component, which can be a metal ion, a coenzyme, or a prosthetic group.
Active Site and Substrate Binding
The enzyme's active site is a specific region on the enzyme where the substrate binds.
It is typically a small portion of the enzyme formed by the unique folding pattern of the protein, which creates a pocket or crevice suitable for the substrate.
The chemical environment within the active site is designed to facilitate the binding of the enzyme to a specific substrate, or substrates, due to its unique amino acid composition.
This results in the formation of an enzyme-substrate complex. The binding is often driven by interactions such as hydrogen bonding and electrostatic forces, contributing to the specificity of substrate attachment.
Once the substrate is bound, a conformational change in the enzyme may occur to better fit the substrate, a concept known as the induced fit model.
After the catalytic reaction, the products are released, and the enzyme is ready to bind to another substrate.