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