metalloendopeptidase inhibitor activity

Definition

Target type: molecularfunction

Binds to and stops, prevents or reduces the activity of metalloendopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain and contain a chelated metal ion at their active sites which is essential to their catalytic activity. [GOC:ai]

Metalloendopeptidase inhibitor activity describes the ability of a molecule to inhibit the catalytic activity of metalloendopeptidases. Metalloendopeptidases are a class of enzymes that catalyze the hydrolysis of peptide bonds within a polypeptide chain. These enzymes are characterized by the presence of a metal ion, typically zinc or cobalt, in their active site. Metalloendopeptidase inhibitors typically bind to the active site of the enzyme, either directly or through an allosteric mechanism, preventing the metal ion from interacting with the substrate. This interaction can block the substrate from binding, preventing the enzyme from cleaving the peptide bond. By inhibiting metalloendopeptidases, these inhibitors can play a crucial role in regulating various biological processes, including protein degradation, signal transduction, and immune response. They have also shown therapeutic potential in the treatment of various diseases, including cancer, Alzheimer's disease, and inflammatory conditions.'
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Proteins (1)

Compounds (1)