Cloned (Comment) | Organism |
---|---|
expression of cDNA in Escherichia coli | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Selenite | recombinant enzyme | Homo sapiens | |
selenium dioxide | recombinant enzyme | Homo sapiens | |
tellurite | 17 mM, 50% non-competitive inhibition of the recombinant enzyme | Homo sapiens | |
tellurium dioxide | 37 mM, 50% inhibition of the recombinant enzyme | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.000014 | - |
reduced NADPH-cytochrome P450 reductase | recombinant enzyme, Km for electron transfer partner NADPH-cytochrone P 450 reductase | Homo sapiens | |
0.3 | - |
FAD | recombinant enzyme | Homo sapiens | |
7.7 | - |
squalene | recombinant enzyme | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(3S)-2,3-epoxy-2,3-dihydrosqualene + FAD + H2O | - |
Homo sapiens | squalene + FADH2 + O2 | - |
r | |
squalene + O2 + AH2 | - |
Homo sapiens | 2,3 oxidosqualene + A + H2O | - |
? | |
squalene + reduced NADPH-cytochrome P450 reductase + O2 | - |
Homo sapiens | (3S)-2,3-epoxy-2,3-dihydrosqualene + oxidized NADPH-cytochrome P450 reductase + H2O | - |
r |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0183 | - |
squalene | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | FAD is loosely bound | Homo sapiens | |
additional information | electron transfer partner NADPH-cytochrome P450 reductase | Homo sapiens |