Protein Variants | Comment | Organism |
---|---|---|
E219A | NMR studies used MMP-12 preserved by E219A substitution of the general base | Homo sapiens |
General Stability | Organism |
---|---|
catalytic domain of MMP-12 exhibits higher activity, more rigidity of its backbone, and lower folding stability than its counterpart of theMMP-3 catalytic domain that has more internal motions throughout | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
DQ-collagen I + H2O | - |
Homo sapiens | ? | - |
? | |
DQ-collagen IV + H2O | - |
Homo sapiens | ? | - |
? | |
elastin fELN-125 + H2O | - |
Homo sapiens | ? | - |
? | |
FS-6 + H2O | - |
Homo sapiens | ? | - |
? | |
triple helical peptide alpha1(V) + H2O | collagen V fibrils | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MMP-3 | - |
Homo sapiens |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.048 | - |
triple helical peptide alpha1(V) | pH 7.5, 25°C, value below | Homo sapiens | |
0.11 | - |
DQ-collagen IV | pH 7.5, 25°C | Homo sapiens | |
0.83 | - |
elastin fELN-125 | pH 7.5, 25°C | Homo sapiens | |
14.04 | - |
DQ-collagen I | pH 7.5, 25°C | Homo sapiens | |
20.63 | - |
FS-6 | pH 7.5, 25°C | Homo sapiens |