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Literature summary for 1.6.2.4 extracted from
- Functional interactions in cytochrome P450BM3. Fatty acid substrate binding alters electron-transfer properties of the flavoprotein domain (1996), Biochemistry, 35, 15029-15037.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| CO | stimulation | Priestia megaterium |  |
| hexadecanol | stimulation | Priestia megaterium | |
| laurate | stimulation | Priestia megaterium | |
| laurate | plus carbon monoxide, greater stimulation compared to laurate alone or carbon monoxide alone, decrease of stimulation in the presence of NADPH | Priestia megaterium | |
| palmitate | stimulation | Priestia megaterium | |
| Tetradecanol | stimulation | Priestia megaterium | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Priestia megaterium |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Priestia megaterium | part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase | ? | - |
? | |
| NADPH + ferricytochrome P450 | Priestia megaterium | during hydroxylation of fatty acids through the bacterial fusion protein P450BM3 | ferrocytochrome P450 + NADP+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Priestia megaterium | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| expressed in Escherichia coli, column chromatography on 2',5'-ADP-agarose | Priestia megaterium |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| oxidation of the reduced P450BM3 by cytochrome c, ferricyanide or 2,6-dichlorophenolindophenol rapidly restores electron transfer and hydroxylase activity | Priestia megaterium |
Storage Stability
| Storage Stability | Organism |
|---|---|
| expressed in E. coli, -80°C | Priestia megaterium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 ferricytochrome c + NADPH | additional electron acceptor: ferricyanide | Priestia megaterium | 2 ferrocytochrome c + NADP+ + H+ | - |
? | |
| 2 ferricytochrome c + NADPH | additional electron acceptor: cytochrome P450 | Priestia megaterium | 2 ferrocytochrome c + NADP+ + H+ | - |
? | |
| 2 ferricytochrome c + NADPH | additional electron acceptor: 2,6-dichlorophenolindophenol | Priestia megaterium | 2 ferrocytochrome c + NADP+ + H+ | - |
? | |
| ferricytochrome c + NADPH + H+ | - |
Priestia megaterium | ferrocytochrome c + NADP+ | - |
r | |
| additional information | simultaneous catalysis of reduction of cytochrome c and hydroxylation of laurate | Priestia megaterium | ? | - |
? | |
| additional information | part of the bacterial fusion protein P450BM3 composed of cytochrome P450 fatty acid hydroxylase and NADPH cytochrome P450 reductase | Priestia megaterium | ? | - |
? | |
| NADPH + ferricytochrome P450 | during hydroxylation of fatty acids through the bacterial fusion protein P450BM3 | Priestia megaterium | ferrocytochrome P450 + NADP+ | - |
? | |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 53.3 | - |
ferricytochrome c | - |
Priestia megaterium | |
| 417 | - |
ferricytochrome c | in the presence of laurate and carbon monoxide | Priestia megaterium | |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Priestia megaterium | |
| FMN | - |
Priestia megaterium | |
| NADPH | - |
Priestia megaterium | |
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