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Revision notes with simplified explanations to understand Enzymes quickly and effectively.
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Enzymes are specialized proteins that function as catalysts, accelerating specific biochemical reactions within the body.
Most enzymes have a globular structure. Within each globule lies a distinct active site, a small crevice or pocket that plays a crucial role in the enzyme's function. This active site has an exact three-dimensional shape tailored to bind with specific molecules, known as substrates. The substrate fits precisely into this site, enabling the enzyme to facilitate the reaction.
Due to the three-dimensional nature of the active site, enzymes can typically catalyze reactions involving only one particular enantiomer of a chiral substrate. This property of enzymes is referred to as stereospecificity.
Enzymes are proteins they speed up reactions and are naturally occurring so they're biological catalysts.
Drugs can be engineered to inhibit a harmful enzyme, preventing it from catalyzing a detrimental reaction.
To achieve this, molecules are developed to closely resemble the shape of the enzyme's natural substrate. These drugs mimic the substrate, binding to the enzyme's active site in its place. By occupying the active site, the drug blocks the actual substrate from binding, effectively preventing the enzyme from catalyzing the reaction. This mechanism is known as enzyme inhibition.
With advances in computer modeling techniques, scientists can now predict the three-dimensional structure of enzymes and other proteins. By understanding the enzyme's shape, they can also deduce the necessary shape of its substrate. This allows for the precise design of inhibitors tailored to the enzyme's specific structure.
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