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Literature summary extracted from
- Sterol biosynthesis by a prokaryote: first in vitro identification of the genes encoding squalene epoxidase and lanosterol synthase from Methylococcus capsulatus (2007), Biosci. Biotechnol. Biochem., 71, 2543-2550.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.17 | Triton X-100 | activates at 0.1% | Methylococcus capsulatus |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.17 | DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3) | Methylococcus capsulatus |
| 5.4.99.7 | expression in Escherichia coli | Methylococcus capsulatus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 5.4.99.7 | 90000 | - |
x * 90000, SDS-PAGE, x * 94000, calculated for thioredoxin-enzyme fusion protein | Methylococcus capsulatus |
| 5.4.99.7 | 94000 | - |
x * 90000, SDS-PAGE, x * 94000, calculated for thioredoxin-enzyme fusion protein | Methylococcus capsulatus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.17 | squalene + reduced cytochrome P450 + O2 | Methylococcus capsulatus | first step in the cyclic chloesterol biosynthesis | (S)-squalene-2,3-epoxide + cytochrome P450 + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.17 | Methylococcus capsulatus | Q603D5 | - |
- |
| 5.4.99.7 | Methylococcus capsulatus | Q603D4 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.17 | squalene + reduced cytochrome P450 + H+ + O2 | absolutely stereo- and regiospecific reaction, co-reaction with NADPH-cytochrome P450 reductase | Methylococcus capsulatus | (3S)-squalene-2,3-epoxide + cytochrome P450 + H2O | - |
? | |
| 1.14.14.17 | squalene + reduced cytochrome P450 + O2 | first step in the cyclic chloesterol biosynthesis | Methylococcus capsulatus | (S)-squalene-2,3-epoxide + cytochrome P450 + H2O | - |
? | |
| 5.4.99.7 | (3S)-2,3-oxidosqualene | reaction is completely regio- and stereospecific | Methylococcus capsulatus | lanosterol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.4.99.7 | ? | x * 90000, SDS-PAGE, x * 94000, calculated for thioredoxin-enzyme fusion protein | Methylococcus capsulatus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.17 | squalene epoxidase | - |
Methylococcus capsulatus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.17 | 25 | - |
assay at | Methylococcus capsulatus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.17 | 7.4 | - |
assay at | Methylococcus capsulatus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.17 | FAD | - |
Methylococcus capsulatus | |
| 1.14.14.17 | reduced cytochrome P450 | - |
Methylococcus capsulatus |
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Release 2023.1 (January 2023)
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