Crucial Role of Active Site in Enzyme Catalysis

Active site

pocket or cleft in the enzyme where the reaction occurs or the specific portion of the enzyme to which a substrate binds during reaction .

The active site is the specific region on an enzyme molecule where substrates bind and undergo chemical reactions. It is a three-dimensional structure that is complementary to the shape of the substrate or substrates involved in the catalyzed reaction.

When a substrate molecule binds to the active site, the enzyme undergoes a conformational change that brings specific amino acids in the active site into position to catalyze the reaction. This can include repositioning of catalytic residues or the creation of an optimal microenvironment for the reaction to occur.

The active site is critical to the function of enzymes because it determines the specificity of the reaction catalyzed by the enzyme. Different enzymes have different active sites, thus allowing them to bind to and catalyze specific substrates. The active site also determines the rate at which the enzyme can carry out its reaction, as well as the overall efficiency of the enzyme.

The active site can be affected by various factors such as the pH, temperature, and the presence of inhibitors or co-factors. Inhibitors may bind to the active site and prevent the substrate from binding or reacting while co-factors may activate the active site and enhance the enzyme activity.

More Answers:

Unlocking the Role of Coenzymes in Cellular Metabolism and Essential Enzyme Function
Unveiling the Role of Cofactors in Enzyme Function: An Overview of Organic and Inorganic Options
Unlocking Enzyme Power: Benefits and Regulation of Proenzymes

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