cysteiniproteaasi

Cysteiniproteaasi, also known as cysteine proteases or thiol proteases, are a class of enzymes that catalyze the hydrolysis of peptide bonds in proteins, specifically those adjacent to cysteine residues. These enzymes are characterized by the presence of a cysteine residue in their active site, which acts as a nucleophile to attack the carbonyl carbon of the peptide bond. This reaction is facilitated by the formation of a covalent intermediate, known as an acyl-enzyme intermediate, which is then hydrolyzed to release the products. Cysteiniproteaasi are found in various organisms, including bacteria, fungi, plants, and animals, and play crucial roles in numerous biological processes, such as protein degradation, cell signaling, and immune response. They are also involved in the pathogenesis of several diseases, including cancer and infectious diseases. Due to their importance in both physiological and pathological processes, cysteiniproteaasi are a major target for drug development, with several inhibitors currently in clinical use or under investigation.