EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.24.B3 | expression of catalytic domain connected to the hemopexin-like domain in Escherichia coli BL21(DE3) | Mus musculus |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
3.4.24.B3 | catalytic domain complexed with a phosphinic inhibitor mimicking the transition state, hanging drop method, 5 mg/ml protein in 0.05 M MES, pH 5.5, 0.5 M ammonium sulfate, 1% v/v trifluoroethanol, 4°C, a few months, X-ray diffraction structure determination at 2.6 A resolution and analysis | Mus musculus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.B3 | phosphinic inhibitor | inhibitor binding mechanism | Mus musculus |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.4.24.B3 | Zinc | 3 zinc atoms per enzyme molecule, metalloproteinase, the zinc binding site is catalytically active | Mus musculus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.B3 | protein + H2O | Mus musculus | - |
peptides | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.24.B3 | Mus musculus | Q02853 | precursor | - |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
3.4.24.B3 | proteolytic degradation of proteins | mechanism | Mus musculus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.24.B3 | protein + H2O | - |
Mus musculus | peptides | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.24.B3 | M10.007 | Merops-ID | Mus musculus |
3.4.24.B3 | matrix metalloproteinase-11 | - |
Mus musculus |
3.4.24.B3 | MMP-11 | - |
Mus musculus |
3.4.24.B3 | SL-3 | - |
Mus musculus |
3.4.24.B3 | ST3 | - |
Mus musculus |