Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme bound to cell surface sulfatide or cholesterol sulfate cleaves specific cell surface proteins and releases similar fragments, whereas the cleavage is not stimulated by cell surface cardiolipin-bound enzyme | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
cardiolipin | associates with the enzyme at the cell surface and inhibits by 92% | Homo sapiens | |
Cholesterol sulfate | associates with the enzyme st the cell surface and modulates the substrate preference of the enzyme, 20% inhibition | Homo sapiens | |
additional information | the internal four residues Ile29, Arg33, Arg51 and Trp55 of MMP-7 are important for binding of inhibitory acidic lipids, overview | Homo sapiens | |
Sulfatide | associates with the enzyme at the cell surface and inhibits by 80% | Homo sapiens | |
TAPI-1 | a hydroxamate-based matrix metalloproteinase inhibitor, reduces the affinity of the enzyme for cholesterol sulfate and cardiolipin, but not for sulfatide, molecular mechanism by which TAPI-1 inhibits binding of MMP-7 to the lipids, overview | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | the enzyme is secreted | Homo sapiens | - |
- |
additional information | the enzyme potentially associates with the cell surface via sulfatide and cardiolipin when they are overexpressed on the cell surface, molecular interaction, overview | Homo sapiens | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P09237 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | recombinant enzyme | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
fibronecin + H2O | pericellular proteolysis | Homo sapiens | ? | - |
? | |
kappa-casein + H2O | - |
Homo sapiens | ? | - |
? | |
laminin-332 + H2O | pericellular proteolysis | Homo sapiens | ? | - |
? | |
additional information | cholesterol sulfate modulates the substrate preference of the enzyme, thereby regulating its pericellular proteolytic action | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Matrix metalloproteinase-7 | - |
Homo sapiens |
MMP-7 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | 37 | assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | 8 | assay at | Homo sapiens |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0006 | - |
pH 8.0, 25°C | Homo sapiens | cardiolipin | |
0.0007 | - |
pH not specified in the publication, 37°C | Homo sapiens | Sulfatide |
General Information | Comment | Organism |
---|---|---|
additional information | the enzyme potentially associates with the cell surface via sulfatide and cardiolipin when they are overexpressed on the cell surface, molecular interaction, overview. The internal four residues Ile29, Arg33, Arg51 and Trp55 of MMP-7 are important for binding of inhibitory acidic lipids, overview | Homo sapiens |
physiological function | matrix metalloproteinases take part in tumor invasion and metastasis through modification of the biological functions of various cell surface proteins and degradation of extracellular matrix proteins. Acidic lipids differentially regulate pericellular proteolysis by MMP-7 through allosteric alteration of the substrate-binding site and their inherent affinities for MMP-7 substrates, overview | Homo sapiens |