3.4.24.65	?	x * 22000, active MMP-12	709415	
3.4.24.65	?	x * 22000, human, SDS-PAGE	31412	
3.4.24.65	?	x * 22000, mature recombinant enzyme without domain I, SDS-PAGE	683327	
3.4.24.65	?	x * 54000, inactive MMP-12 protenzyme, SDS-PAGE	-, 683054	
3.4.24.65	?	x * 54000, inactive proenzyme, x * 45000, intermediate enzyme	683217	
3.4.24.65	?	x * 54000, inactive proenzyme, x * 45000, intermediate enzyme, x * 22000, mature active enzyme	671345	
3.4.24.65	?	x * 54000, pro-MMP-12, x * 22000, active mature MMP-12	708452	
3.4.24.65	?	x * 54000, pro-MMP-12, x * 29000, mature active MMP-12	708303	
3.4.24.65	monomer	1 * 22000, mouse, form B and C, SDS-PAGE	31409	
3.4.24.65	additional information	MMP-12 is synthesized as 54-kDa proenzyme that is processed into a 45-kDa and then a 22-kDa active form	671345	
3.4.24.65	additional information	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	additional information	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	additional information	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	additional information	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