- Metalloproteinase
-
Metalloproteinases (or metalloproteases) constitute a family of enzymes from the group of proteases, classified by the nature of the most prominent functional group in their active site. These are proteolytic enzymes whose catalytic mechanism involves a metal. Most metalloproteases are zinc-dependent, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands co-ordinating the metal ion can vary with histidine, glutamate, aspartate, lysine and arginine. The fourth coordination position is taken up by a labile water molecule.
There are two subgroups of metalloproteinases:
- exopeptidases: metalloexopeptidases (EC number: 3.4.17).
- endopeptidases: metalloendopeptidases (3.4.24). Well known metalloendopeptidases include ADAM proteins and matrix metalloproteinases.
Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator which removes zinc, which is essential for activity. They are also inhibited by the chelator orthophenanthroline.
External links
- The MEROPS online database for peptidases and their inhibitors: Metallo Peptidases
- MeSH Metalloproteases
- Metalloproteinase at eMedicine Dictionary
- Proteopedia: Metalloproteases
See also
- Matrix metalloproteinase
- The Proteolysis Map
3.4.21-24: Endopeptidase Serine proteases · Cysteine protease · Aspartic acid protease · Metalloendopeptidases
Other/ungrouped: Amyloid precursor protein secretase (Alpha secretase, Beta-secretase 1, Beta-secretase 2, Gamma secretase)3.4.99: Unknown Categories:- EC 3.4.24
- EC 3.4.17
- Hydrolase stubs
Wikimedia Foundation. 2010.
