Metallopeptidázok

Metallopeptidázok are a class of enzymes that catalyze the hydrolysis of peptide bonds and require a metal ion, typically zinc, for their catalytic activity. These enzymes are found in a wide variety of organisms, from bacteria to humans, and play crucial roles in numerous biological processes. Their substrates are proteins, and they are involved in functions such as protein degradation, blood clotting, digestion, and cell signaling.

The defining characteristic of metallopeptidázok is their reliance on a metal cofactor. This metal ion is usually coordinated within the active site of the enzyme and interacts with key amino acid residues, such as histidine and glutamate. This metal-peptide-water complex is essential for the catalytic mechanism, which typically involves the activation of a water molecule to perform nucleophilic attack on the peptide bond.

Metallopeptidázok are further classified based on their substrate specificity and structural features. Some are exopeptidases, cleaving amino acids from the ends of a peptide chain, while others are endopeptidases, hydrolyzing internal peptide bonds. Examples of metallopeptidázok include matrix metalloproteinases (MMPs), angiotensin-converting enzyme (ACE), and thermolysin. Due to their involvement in diverse physiological and pathological processes, metallopeptidázok are also targets for drug development, with inhibitors being used to treat conditions ranging from inflammation to cancer.