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Literature summary extracted from
- Structure of a cytochrome P450-redox partner electron-transfer complex (1999), Proc. Natl. Acad. Sci. USA, 96, 1863-1868.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.14.1 | crystal structure of the complex between the heme- and FMN-binding domains of the enzyme, crystals are grown at room temperature by liquid-liquid free interface diffusion in a capillary, the flavodoxin-like flavin domain is positioned at the proximal face of the heme domain | Priestia megaterium |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.1 | Priestia megaterium | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.1 | additional information | self-sufficient fatty acid monooxygenase | Priestia megaterium | ? | - |
? |  |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.1 | CYP102 | - |
Priestia megaterium |
| 1.14.14.1 | cytochrome P-450 BM3 | - |
Priestia megaterium |
| 1.14.14.1 | flavocytochrome P450BM-3 | - |
Priestia megaterium |
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Release 2023.1 (January 2023)
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