Application | Comment | Organism |
---|---|---|
drug development | MMP-9 is a therapeutic target in autoimmune diseases, vascular pathologies, and cancer | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression of full-length pro-MMP-9 in Spodoptera frugiperda Sf9 cells | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | a zinc endopeptidase | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | MMP-9 contains a heavily O-glycosylated OG domain | Homo sapiens |
Purification (Comment) | Organism |
---|---|
recombinant full-length pro-MMP-9 from Spodoptera frugiperda Sf9 cells | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | varied enzyme conformations and in facilitating independent movements of the terminal domains may endorse recognition, binding, and processing of substrates, ligands, as well as receptors and marks this domain as an additional target for the design of selective regulators, overview | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | dimers of MMP-9 are detected under physiological conditions | Homo sapiens |
More | the recombinant enzyme forms mixtures of monomers and other higher oligomeric species, structural model of multidomain full-length pro-MMP-9, including the unique proline-rich and heavily O-glycosylated OG domain, combining small-angle X-ray scattering with single-molecule atomic force microscopy imaging to characterize a full-length structural model of pro-MMP-9, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
matrix metalloproteinase-9 | - |
Homo sapiens |
MMP-9 | - |
Homo sapiens |
pro-matrix metalloproteinase-9 | - |
Homo sapiens |