serine-type peptidase activity

Definition

Target type: molecularfunction

Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). [https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE]

Serine-type peptidase activity is a catalytic activity that involves the hydrolysis of peptide bonds. This type of enzymatic activity is crucial in a wide range of biological processes, including protein degradation, signal transduction, and immune responses. The mechanism of serine-type peptidase activity involves the formation of a tetrahedral intermediate, which is stabilized by the catalytic triad of amino acids, typically consisting of serine, histidine, and aspartate. The serine residue in the active site acts as a nucleophile, attacking the carbonyl carbon of the peptide bond. The histidine residue acts as a base, deprotonating the serine hydroxyl group, and the aspartate residue stabilizes the histidine residue. The resulting tetrahedral intermediate is then broken down, releasing the carboxyl-terminal portion of the peptide and leaving the amino-terminal portion bound to the enzyme. This process is repeated until the peptide is completely hydrolyzed. Serine peptidases are found in all living organisms and are classified into different families based on their structural features and catalytic mechanisms. Some examples of serine peptidases include chymotrypsin, trypsin, and elastase, which play important roles in digestion, and subtilisin, which is used in various industrial applications. Serine peptidases are also involved in disease processes, such as cancer and Alzheimer's disease, making them targets for drug development. '
"

Proteins (37)

Compounds (285)