Ad
related to: mmp 13 enzyme blockers names chart
Search results
Results From The WOW.Com Content Network
[5] [6] It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. [7] MMP-13 has a predicted molecular weight around 54 kDa. [8] It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain . Although the actual ...
5-(spiropyrrolidin-5-yl)pyrimidinetrione is a compound named 848773-43-3 that is a potent MMP-2, MMP-9 and MMP-13 inhibitor that spares MMP-1 and TACE. By substituting 1,3,4-oxadiazol-2-yl heteroaryl at C-4’ of the diphenylether segment to accomplish MMP-13 selectivity over MT-1 MMP, made the compound 420121-84-2.
A matrix metalloproteinase inhibitor (INN stem –mastat [1]) inhibits matrix metalloproteinases.Because they inhibit cell migration, they have antiangiogenic effects. They are endogenous or exogenous.
Matrix metalloproteinases (MMPs), also known as matrix metallopeptidases or matrixins, are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; [1] other family members are adamalysins, serralysins, and astacins.
This page was last edited on 9 February 2024, at 00:17 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.
ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13)—also known as von Willebrand factor-cleaving protease (VWFCP)—is a zinc-containing metalloprotease enzyme that cleaves von Willebrand factor (vWf), a large protein involved in blood clotting.
Top: enzyme (E) accelerates conversion of substrates (S) to products (P). Bottom: by binding to the enzyme, inhibitor (I) blocks binding of substrate. Binding site shown in blue checkerboard, substrate as black rectangle, and inhibitor as green rounded rectangle. An enzyme inhibitor is a molecule that binds to an enzyme and blocks its activity.
The MMP family is formed by twenty related zinc-dependent enzymes. They are noted for having the ability to degrade extracellular matrix proteins, such as collagens , laminin , and proteoglycans . These calcium- and zinc-dependent proteases are activated at neutral pH and twenty-three have been found present in mammalian cells.