Metalloprotease
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See: Metalloprotease Enzyme, Metalloprotease Enzyme Family.
References
- (Wikipedia, 2009) ⇒ http://en.wikipedia.org/wiki/Metalloprotease
- Metalloproteinases (or metalloproteases) constitute a family of enzymes from the group of proteinases, 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.
- Gene Ontology http://amigo.geneontology.org/cgi-bin/amigo/term-details.cgi?term=GO:0008237&session_id=3029amigo1244034791
- Accession: GO:0008237
- Ontology: molecular function
- Synonyms
- exact: metalloprotease activity
- exact: metalloproteinase activity
- Definition
- Catalysis of the hydrolysis of peptide bonds by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. [source: GOC:mah, http://merops.sanger.ac.uk/about/about_9.htm#CATTYPE]