Metalloprotease inhibitor

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There are three classes of commonly used inhibitors for metalloproteinases.

• In vitro, EDTA, 1,10-phenanthroline and other chelating compouds lower the concentration of metal to the point where the metal is removed from the enzyme active site.

• Classical lock and key inhibitors such as phosphoramidon and bestatin bind tightly by approximating the transition state of the hydrolysis of the peptide, preventing it from acting on other substrates.

• Protein inhibitors such as α2-macroglobulin are known to work with metalloproteinases.

[edit] References

• Sigma Aldrich Catalog