EC Number   |
Inhibitors |
Structure |
|---|
   3.4.24.22 | 1,10-phenanthroline |
- |
   |
| 3.4.24.22 | DTT |
- |
|
| 3.4.24.22 | EDTA |
- |
|
| 3.4.24.22 | EGTA |
- |
|
| 3.4.24.22 | GM6001 |
a broad-spectrum MMP inhibitor |
|
| 3.4.24.22 | more |
the endogenous tissue inhibitors of metalloproteinases (TIMPs) regulate proteolytic activity by binding tightly to the MMP active site. While each of the four TIMPs can inhibit most MMPs, binding data reveal tremendous heterogeneity in affinities of different TIMP/MMP pairs. Identification of a group of highly conserved contacts at the heart of MMP/TIMP complexes that define the conserved mechanism of inhibition, as well as a second category of diverse adventitious contacts at the periphery of the interfaces |
|
| 3.4.24.22 | N-isobutyl-N-(4-methoxy-phenylsulfonyl)glycyl hydroxamic acid |
i.e. NNGH, study of binding mode. Interaction of inhibitor with Zn1 atom and S1 subsite |
|
| 3.4.24.22 | PAI-1 |
functions as an upstream regulator of a MMP-10-initiated collagenolytic phenotype, it blocks conversion of MMP-10 to its active form. Neutralization of endogenous PAI-1 with function blocking antibodies accelerates both collagenolysis and activation of MMP-10 |
|
| 3.4.24.22 | Specific tissue inhibitor of metalloproteinases |
TIMP-1 |
|
| 3.4.24.22 | Specific tissue inhibitor of metalloproteinases |
- |
|
