Architecture and function of metallopeptidase catalytic domains.

@article{CerdCosta2014ArchitectureAF,
  title={Architecture and function of metallopeptidase catalytic domains.},
  author={N{\'u}ria Cerd{\`a}-Costa and F Xavier Gomis-R{\"u}th},
  journal={Protein science : a publication of the Protein Society},
  year={2014},
  volume={23 2},
  pages={
          123-44
        }
}
The cleavage of peptide bonds by metallopeptidases (MPs) is essential for life. These ubiquitous enzymes participate in all major physiological processes, and so their deregulation leads to diseases ranging from cancer and metastasis, inflammation, and microbial infection to neurological insults and cardiovascular disorders. MPs cleave their substrates without a covalent intermediate in a single-step reaction involving a solvent molecule, a general base/acid, and a mono- or dinuclear catalytic… CONTINUE READING

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