Matrix Metalloproteinase 12: Difference between revisions
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Furthermore, researchers have successfully produced synthetic inhibitors : These inhibitors contain a chelating group, which binds the catalytic zinc atom involved in the catalytic site. Common chelating groups include hydroxamates, carboxylates, thiols, and phosphinyls. Hydroxymates are particularly potent inhibitors of MMPs thanks to their bidentate chelation of the zinc atom. A 2oxu inhibitor can also inhibit other MMPs after a few modifications : Only the substituents interacting with the pocket have to be modified because of the various binding pockets of the MMPs. | Furthermore, researchers have successfully produced synthetic inhibitors : These inhibitors contain a chelating group, which binds the catalytic zinc atom involved in the catalytic site. Common chelating groups include hydroxamates, carboxylates, thiols, and phosphinyls. Hydroxymates are particularly potent inhibitors of MMPs thanks to their bidentate chelation of the zinc atom. A 2oxu inhibitor can also inhibit other MMPs after a few modifications : Only the substituents interacting with the pocket have to be modified because of the various binding pockets of the MMPs. | ||
That means that from a a single inhibitor, researchers are able to create more or less specificity toward several enzymes. | That means that from a a single inhibitor, researchers are able to create more or less specificity toward several enzymes. | ||
==3D structures of matrix metalloproteinase == | |||
[[Matrix metalloproteinase]] | |||
== References == | == References == | ||
