The active site of an enzyme is the location of the enzyme. The substrate molecules bind and a chemical reaction takes place in the active site. The active site develops by amino acid residues. Amino acid establishes temporary bonds with the substrate as well as residues that catalyze the substrate’s reaction.
Although, the active site of an enzyme only takes up 10–20 percent volume of an enzyme. It is the most critical component because it catalyzes the chemical process directly.
However, the other amino acids inside the protein are essential to maintain the tertiary structure of the enzymes. They normally comprise 3 to 4 amino acids.
High specificity achieves by optimizing each active site to bind a single substrate and catalyze a specific reaction. The structure of the substrates and the positioning of amino acids within the active site of an enzyme dictate this specificity.
To perform their functions, enzymes often need to bind with co-factor.
Typically, an enzyme molecule contains only two active sites, each of which is exclusive to one type of substrate. A binding site in an active site binds the substrate and positions it for catalysis.
The active sites are frequently enzyme grooves or pockets. The enzyme grooves or pockets find deep inside the enzymes or between the surfaces of multimeric enzymes.
However, the residues do not transform at the end of the process. Active sites can catalyze a reaction multiple times. It accomplishes by lowering the activation energy of the reaction, allowing for more substrates to take action in the reaction.
Active Site Lock and Key Theory of an enzyme
This theory is analogous to the Lock and Key Theory, except that the site is preprogrammed to bind to the substrate properly in the transition state instead of the ground state. The development of a transition state in a solution necessitates a significant amount of energy to move solvent molecules, slowing the reaction.
As a result, the Active site of an enzyme can substitute solvent molecules and enclose the substrates to reduce the solution’s counterproductive influence. The active site’s availability of charged groups engages substrates and ensures electrostatic complementarity.