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 (Comment) | Organism |
---|---|
expression in Escherichia coli | Priestia megaterium |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Priestia megaterium | - |
- |
- |
Purification (Comment) | Organism |
---|---|
expressed in Escherichia coli, column chromatography on 2',5'-ADP-agarose | Priestia megaterium |
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 | Organism |
---|---|
expressed in E. coli, -80°C | Priestia megaterium |
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 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 | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Priestia megaterium | |
FMN | - |
Priestia megaterium | |
NADPH | - |
Priestia megaterium |