The active site is usually a small pocket at the surface of the enzyme that contains residues responsible for the substrate specificity (charge, hydrophobicity, steric hindrance) and catalytic residues which often act as proton donors or acceptors or are responsible for binding a cofactor such as PLP, TPP or NAD. The active site is also the site of inhibition of enzymes (see Enzyme inhibitor article).
There are several models of how enzymes work: the lock-and-key model and the induced fit model. Substrates bind to the active site of the enzyme or a specificity pocket through hydrogen bonds, hydrophobic interactions, temporary covalent bond or a combination of all of these to form the enzyme-substrate complex. Residues of the active site will act as donors or acceptors of protons or other groups on the substrate to facilitate the reaction. In other words, the active site modifies the reaction mechanism in order to decrease the activation energy of the reaction. The product is usually unstable in the active site due to steric hindrances that force it to be released and return the enzyme to its initial state.
|Topics||Active site - Allosteric regulation - Binding site - Catalytically perfect enzyme - Coenzyme - Cofactor - Cooperativity - EC number|
Enzyme catalysis - Enzyme inhibitor - Enzyme kinetics - Lineweaver-Burk plot - Michaelis-Menten kinetics - List of enzymes
|Types||EC1 Oxidoreductases/list - EC2 Transferases/list - EC3 Hydrolases/list - EC4 Lyases/list - EC5 Isomerases/list - EC6 Ligases/list|
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