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Literature summary extracted from
- Cloning sequencing and expression of the gene for cytochrome P450meg, the steroid-15 beta-monooxygenase from Bacillus megaterium ATCC 13368 (1993), Mol. Gen. Genet., 241, 170-176.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.15.8 | expressed in Escherichia coli and Bacillus subtilis. No hydroxylation is found with protein extracts from recombinant Escherichia coli strains since cytochrome P450meg needs additional electron transfer proteins for enzymatic activity, which are missing in Escherichia coli. Bacillus subtilis, in contrast to Escherichia coli, contains an electron transfer system capable of supporting the activity of cytochrome P450meg | Priestia megaterium |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.15.8 | Priestia megaterium | Q06069 | ATCC 13368 | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.15.8 | 6alpha-fluoro-16alpha-methyl-deoxycorticosterone + reduced ferredoxin + O2 | - |
Priestia megaterium | 15beta-hydroxy-6alpha-fluoro-16alpha-methyl-deoxycorticosterone + oxidized ferredoxin + H2O | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.15.8 | cytochrome P450meg | - |
Priestia megaterium |
| 1.14.15.8 | steroid-15-beta-monooxygenase | - |
Priestia megaterium |
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