Metalloprotease inhibitor
Metalloprotease inhibitors are cellular inhibitors of the matrix metalloprotease (or metalloproteinase) family of proteins (MMP). Several other proteins have similar inhibitory effects, however none as effective (netrins, procollagen C-terminal proteinase enhancer (PCPE), reversion-inducing cysteine-rich protein with Kazal motifs (RECK) and tissue factor pathway inhibitor (TFPI-2)). They might have other biological activities which have yet been fully characterised.[1]
There are three classes of commonly used inhibitors for metalloproteinases.
- In vitro, EDTA, 1,10-phenanthroline and other chelating compounds 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.
References
- ↑ Baker, Andrew; Dylan R. Edwards; Gillian Murphy (October 2002). "Metalloproteinase inhibitors: biological actions and therapeutic opportunities". J Cell Sci 115: 3719–3727. doi:10.1242/jcs.00063. Retrieved 19 February 2013.
External links
This article is issued from Wikipedia - version of the Monday, July 13, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.