Handling Metalloproteinases

Current Protocols in Protein Science
Sven FridrichWalter Stöcker

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.

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Citations

Mar 27, 2018·Molecular Reproduction and Development·Kimberly StephensCatherine D Thaler
Sep 13, 2019·Expert Opinion on Therapeutic Patents·Silvia Bua, Claudiu T Supuran
Oct 21, 2020·International Journal of Biological Macromolecules·Pan LiuJing Jin

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