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Literature summary extracted from
- Purification and characterization of recombinant squalene epoxidase (1995), J. Lipid Res., 36, 1489-1497.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.17 | additional information | 105000 g supernatant, 8.5fold activation of microsomal enzyme, 3fold activation of N-terminal truncated recombinant enzyme | Rattus norvegicus | |
| 1.14.14.17 | NADPH cytochrome c reductase | required for activity of N-terminal truncated recombinant enzyme in a concentration-dependent manner | Rattus norvegicus | |
| 1.14.14.17 | Triton X-100 | 0.1%, 36fold activation of microsomal enzyme, 0.05%, 34fold activation of N-terminal truncated recombinant enzyme | Rattus norvegicus |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.17 | expression of cDNA in Escherichia coli | Rattus norvegicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.17 | NB-598 | 0.0000032 mM, 50% inhibition of microsomal enzyme, 0.0000019 mM, 50% inhibition of N-terminal truncated recombinant enzyme | Rattus norvegicus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.17 | 0.0036 | - |
squalene | N-terminal truncated recombinant enzyme | Rattus norvegicus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.17 | Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.17 | recombinant enzyme, Ni-NTA-agarose, Blue Sepharose CL-6B | Rattus norvegicus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.17 | 0.17 | - |
N-terminal truncated recombinant enzyme | Rattus norvegicus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.17 | 2,3-oxidosqualene + NADPH + O2 | N-terminal truncated recombinant enzyme | Rattus norvegicus | 2,3,22,23-dioxidosqualene + NADP+ + H2O | - |
? | |
| 1.14.14.17 | squalene + NAD(P)H + O2 | - |
Rattus norvegicus | (S)-squalene-2,3-epoxide + NADP+ + H2O | - |
? | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.17 | 7.5 | 8.5 | microsomal and N-terminal truncated recombinant enzyme | Rattus norvegicus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.17 | FAD | required for activity | Rattus norvegicus | |
| 1.14.14.17 | additional information | neither FMN nor riboflavin can replace FAD | Rattus norvegicus |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.17 | 0.00000041 | - |
NB-598 | N-terminal truncated recombinant enzyme | Rattus norvegicus | |
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