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, some use cobalt. The metal ion is coordinated to the protein via three histadine imidazole ligands. 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
- MeSH Metalloproteases
- Metalloproteinase at eMedicine Dictionary
- Proteopedia: Metalloproteases
See also
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