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RESEARCH PRODUCT
Handling Metalloproteinases.
Sven FridrichWalter StöckerKonstantin Karmilinsubject
0301 basic medicineMetal ions in aqueous solutionGlutamic AcidMatrix metalloproteinaseHydrogen-Ion ConcentrationBiochemistryCombinatorial chemistryCatalysisMetal03 medical and health scienceschemistry.chemical_compoundZinc030104 developmental biologychemistryStructural Biologyvisual_artvisual_art.visual_art_mediumMetalloproteasesMoleculeImidazolePeptide bondAnimalsHumansAstacinHistidinedescription
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. © 2016 by John Wiley & Sons, Inc. Keywords: metzincin; MMP; ADAM; ADAMTS; astacin; meprin; tolloid
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2016-02-03 | Current protocols in protein scienceLiterature Cited |