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Literature summary extracted from
- Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase (2000), Arch. Biochem. Biophys., 374, 381-388.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.17 | expression of cDNA in Escherichia coli | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.17 | Selenite | recombinant enzyme | Homo sapiens |  |
| 1.14.14.17 | selenium dioxide | recombinant enzyme | Homo sapiens | |
| 1.14.14.17 | tellurite | 17 mM, 50% non-competitive inhibition of the recombinant enzyme | Homo sapiens | |
| 1.14.14.17 | tellurium dioxide | 37 mM, 50% inhibition of the recombinant enzyme | Homo sapiens | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.17 | 0.000014 | - |
reduced NADPH-cytochrome P450 reductase | recombinant enzyme, Km for electron transfer partner NADPH-cytochrone P 450 reductase | Homo sapiens | |
| 1.14.14.17 | 0.3 | - |
FAD | recombinant enzyme | Homo sapiens | |
| 1.14.14.17 | 7.7 | - |
squalene | recombinant enzyme | Homo sapiens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.17 | Homo sapiens | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.17 | recombinant enzyme | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.14.17 | liver | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.17 | (3S)-2,3-epoxy-2,3-dihydrosqualene + FAD + H2O | - |
Homo sapiens | squalene + FADH2 + O2 | - |
r | |
| 1.14.14.17 | squalene + O2 + AH2 | - |
Homo sapiens | 2,3 oxidosqualene + A + H2O | - |
? | |
| 1.14.14.17 | 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 [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.17 | 0.0183 | - |
squalene | - |
Homo sapiens | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.17 | FAD | FAD is loosely bound | Homo sapiens | |
| 1.14.14.17 | additional information | electron transfer partner NADPH-cytochrome P450 reductase | Homo sapiens |
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