title: Handling Metalloproteinases.
abstract: Substrate cleavage by metalloproteinases involves nucleophilic attack on the scissile peptide bond by a water molecule that is polarized by a catalytic metal, usually a zinc ion, and a general base, usually the carboxyl group of a glutamic acid side chain. The zinc ion is most often complexed by imidazole nitrogens of histidine side chains. This arrangement suggests that the physiological pH optimum of most metalloproteinases is in the neutral range. In addition to their catalytic metal ion, many metalloproteinases contain additional transition metal or alkaline earth ions, which are structurally important or modulate the catalytic activity. As a consequence, these enzymes are generally sensitive to metal chelators. Moreover, the catalytic metal can be displaced by adventitious metal ions from buffers or biological fluids, which may fundamentally alter the catalytic function. Therefore, handling, purification, and assaying of metalloproteinases require specific precautions to warrant their stability.
authors.affiliation: Johannes Gutenberg University Mainz, Institute of Zoology, Cell and Matrix Biology, Germany.
authors.forename: Sven
authors.initials: S
authors.lastname: Fridrich
authors.affiliation: Johannes Gutenberg University Mainz, Institute of Zoology, Cell and Matrix Biology, Germany.
authors.forename: Konstantin
authors.initials: K
authors.lastname: Karmilin
authors.affiliation: Johannes Gutenberg University Mainz, Institute of Zoology, Cell and Matrix Biology, Germany.
authors.forename: Walter
authors.initials: W
authors.lastname: Stöcker
mesh_terms: D000818:Animals; D002384:Catalysis; D018698:Glutamic Acid / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D045726:Metalloproteases / Q000737:chemistry* / Q000378:metabolism; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism
chemical_list: D018698:Glutamic Acid; D045726:Metalloproteases; D015032:Zinc
keywords: ADAM; ADAMTS; MMP; astacin; meprin; metzincin; tolloid
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