EC Number   |
Subunits |
Reference |
|---|
   3.4.24.65 | More |
NMR and mass spectrometry structure determination and anaylsis of the MMP-12 catalytic domain using the refolded recombinantly expressed protein, overview |
684029 |
| 3.4.24.65 | More |
NMR structure determination and analysis of unprocessed enzyme mutant E219A in absence of inhibitor, comparison to the enzyme crystal structure, PDB code 1JK3, active site structure, overview |
683781 |
| 3.4.24.65 | More |
pro-MMP-12 contains an N-terminal pro-domain, a catalytic domain, and a C-terminal hemopexin-like domain. The pro-domain is cleaved during maturation. The catalytic domain is essential for the substrate-converting activities of MMPs. Since MMP12 without C-terminal domain is still enzymatically active, the MMP12 C-terminal domain seems not to be required for substrate catalysis. A peptide sequence in the C-terminal domain is responsible for the anti-bacterial activity of MMP-12, but the catalytic domain is not required for the bactericidal property of MMP12, overview |
709559 |
| 3.4.24.65 | More |
the antimicrobial properties of MMP12 do not reside within its catalytic domain, but rather within the carboxy-terminal domain, which contains a unique four amino acid sequence on an exposed beta loop of the protein that is required for the observed antimicrobial activity, within the sequence designated SR-20, i.e. 344-SRNQLFLFKDEKYWLINNLV-363. Three-dimensional homology modeling of mouse MMP12 C-terminal domain, overview |
710050 |
