Active site
(Redirected from Catalytic domain)
Active Site
The active site is a region on an enzyme where the substrate binds and where the catalytic action occurs. It is a key component in the enzyme-substrate complex, a temporary molecule formed when an enzyme comes into perfect contact with its substrate.
Structure[edit | edit source]
The active site is typically a groove or pocket formed by the amino acid residues that make up the enzyme's structure. This site is usually found in a deep groove or pocket on the enzyme surface, ensuring that the reaction can take place in an optimal environment, isolated from the rest of the cell.
Function[edit | edit source]
The function of the active site is to bind the substrate and catalyze its conversion into the product. This is achieved through a series of steps known as the catalytic cycle. The active site provides a unique microenvironment within the enzyme, facilitating the reaction and ensuring specificity.
Mechanism[edit | edit source]
The mechanism of the active site involves several stages, including substrate binding, transition state facilitation, and product release. The active site achieves this through a variety of mechanisms, including acid-base catalysis, covalent catalysis, and metal ion catalysis.
Active Site and Enzyme Specificity[edit | edit source]
The specificity of an enzyme for its substrate is due to the precise interaction of the active site and the substrate. This interaction is based on the lock and key model or the induced fit model, both of which describe how enzymes and substrates interact.
Inhibition[edit | edit source]
Enzyme inhibitors can bind to the active site, preventing the normal substrate from binding and thus inhibiting the enzyme's function. These inhibitors can be competitive, non-competitive, or uncompetitive, depending on their mechanism of action.
See Also[edit | edit source]
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Contributors: Prab R. Tumpati, MD