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Results 1 - 10 of 21 > >>
EC Number Activating Compound Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.244-aminophenylmercuric acetate - 651301
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24aminophenylmercuric acetate - 683842
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24heparan sulfate essential for thrombin-mediated activation of pro-MMP-2 717813
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24interleukin 1beta increases enzyme expression and activity in cardiac microvascular endothelial cells, involvement of PKC and/or MAPK signaling cascades, overview, the activation is inhibited by 52% by GΓΆ6976, a PKC inhibitor, at 100 nM, while inhibitors SN50 and SP600125 have no effect on the activation 683045
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24membrane-type 1 matrix metalloproteinase activity in the extracellular environment is modulated by this activator 653934
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24MMP-14 MMP-14 activates MMP-2 during degeneration of invertebral disc, a major activation pathway of MMP-2 involves complex formation with MMP-14 and a tissue inhibitor of metalloproteinases-2, TIMP-2, overview 683804
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24more a complex formed by MT1-MMP, TIMP-2, and MMP-2 and located at the cell surface, is involved in MMP-2 activation, overview 683846
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24more activation of pro-MMP-2 by 4-aminophenylmercuric acetate 683230
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24more heparan sulfate is required for thrombin-mediated activation of pro-MMP-2 by binding to thrombin, presumably through conformational changes at the active site of the enzyme. Homodimerization of the enzyme enhances thrombin-mediated activation of pro-MMP-2. Enzyme residue Cys102 plays a role in inhibition of catalytic activity through a cysteine-zinc ion pairing, this pairing is disrupted by the intermolecular disulfide bond in the MMP-2 homodimer, resulting in enzyme activation. Disruption of the cysteine-zinc ion pairing by homodimerization of MMP-2 opens the active site, but it may accommodate only small peptide substrates. Thus, MMP-2 propeptide processing is a prerequisite to gain its proteolytic activity against large substrates, including gelatin 734182
Display the word mapDisplay the reaction diagram Show all sequences 3.4.24.24more implantation of 9L glioma cells into brain increases the expression of MMP-2, overview 683427
Results 1 - 10 of 21 > >>