EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.24.24 | more |
activation of pro-MMP-2 by 4-aminophenylmercuric acetate |
683230 |
| 3.4.24.24 | more |
artificial biotinylation of the purified recombinant CBD domain for library screening, overview |
683140 |
| 3.4.24.24 | phosphoprotein |
proMMP-2 contains 29 potential phosphorylation sites, that at least five of these sites are phosphorylated, purified MMP-2 is phosphorylated by protein kinase C in vitro, peptide mass fingerprint for phosphorylation site determination, overview |
683452 |
| 3.4.24.24 | proteolytic modification |
activation |
683427 |
| 3.4.24.24 | proteolytic modification |
activation of 72 kDa proenzyme by aminophenyl-mercuric acetate to 62 and 45 kDa species, no spontaneous autoactivation |
670231 |
| 3.4.24.24 | proteolytic modification |
activation of pro-MMP-2 with 1 mM APMA (p-aminophenylmercuric acetate) for 1 h at 37°C, in buffer containing 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10 mM CaCl2, and 0.05% Brij L23 |
755324 |
| 3.4.24.24 | proteolytic modification |
activation of pro-MMP2 to MMP-2 |
752440 |
| 3.4.24.24 | proteolytic modification |
concanavalin A induces the enzyme activation through membrane type 1 matrix metalloprotease from 72 kDA proenzyme to 62 kDa active enzyme in the non-pigmented ciliary epithelial cells and fibroblast from periodontal ligaments |
733040 |
| 3.4.24.24 | proteolytic modification |
membrane type MMP-1, MT1-MMP, participates in the activation of gelatinase A, overview |
668208 |
| 3.4.24.24 | proteolytic modification |
p-aminophenylmercuric acetate (APMA) promotes activation of pro-MMP2 and its autocatalysis to active MMP2 |
752440 |
