matriisimetalloproteaasit

Matriisimetalloproteaasit refers to a class of enzymes belonging to the peptidase family M. These enzymes are involved in the processing and modification of proteins, particularly metal-containing proteins.

They are metal-dependent hydrolases, meaning their catalytic activity is facilitated by the presence of metal ions such as zinc or magnesium. In their catalytic site, these enzymes utilize a specific arrangement of metal ions and proline residues to hydrolyze metal-protein complexes.

The distinct site within substrate proteins, where these enzymes recognize and bind their substrates, is rich in beta-branched isoleucine or valine residues. Members of this class are predominantly extracellular enzymes, responsible for the clearance of proteins that contain metal ions from the body's circulation.

Their normal physiological function includes the removal of proteins with attached metal ions, as an evolution survival mechanism to cope with unwanted metal complexes harm the necessary biological element proteins or lead. Dysregulation of this family of enzymes has been implicated in neurodegenerative disorders and certain types of Alzheimer's disease.

Variations in matriisimetalloproteaasit can be broken down into different subcategories, based primarily on the possible substrate types or tissue distribution patterns of the subunits within the different tissue or protein architectures. Matriisimetalloproteaasit can be affected by '-chemical misconstruction degradation of metabolism, correcting it with millisecond improvements'