EC Number | Application | Comment | Organism |
---|---|---|---|
1.14.14.11 | synthesis | construcution of fusion proteins that join the C-terminus of the epoxidase StyA to the N-terminus of FAD reductase StyB through a linker peptide and application in the synthesis of of a broad range of substituted indoles to indigoid chromophores. The fusion proteins are self-regulated and couple efficiently NADH oxidation to styrene epoxidation | Rhodococcus opacus |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.14.11 | - |
Rhodococcus opacus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.14.11 | additional information | construcution of fusion proteins that join the C-terminus of the epoxidase StyA to the N-terminus of FAD reductase StyB through a linker peptide and application in the synthesis of of a broad range of substituted indoles to indigoid chromophores. The fusion proteins are self-regulated and couple efficiently NADH oxidation to styrene epoxidation | Rhodococcus opacus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.11 | Rhodococcus opacus | A0A076JVU4 | isoform StyA | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.11 | 1-methylindole + FADH2 + O2 | - |
Rhodococcus opacus | 1-methyl-1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? | |
1.14.14.11 | 1-methylindole-5-carboxylate + FADH2 + O2 | - |
Rhodococcus opacus | 1-methyl-3-oxo-2,3-dihydro-1H-indole-5-carboxylic acid + FAD + H2O | - |
? | |
1.14.14.11 | 4-methoxyindole + FADH2 + O2 | - |
Rhodococcus opacus | 4-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? | |
1.14.14.11 | 5-methoxyindole + FADH2 + O2 | - |
Rhodococcus opacus | 5-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? | |
1.14.14.11 | 6-bromoindole + FADH2 + O2 | - |
Rhodococcus opacus | 6-bromo-1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? | |
1.14.14.11 | 6-chloroindole + FADH2 + O2 | - |
Rhodococcus opacus | 6-chloro-1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? | |
1.14.14.11 | 6-methoxyindole + FADH2 + O2 | - |
Rhodococcus opacus | 6-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? | |
1.14.14.11 | 7-azaindole + FADH2 + O2 | - |
Rhodococcus opacus | 1,2-dihydro-3H-pyrrolo[2,3-b]pyridin-3-one + FAD + H2O | - |
? | |
1.14.14.11 | 7-methoxyindole + FADH2 + O2 | - |
Rhodococcus opacus | 7-methoxy-1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? | |
1.14.14.11 | indole + FADH2 + O2 | - |
Rhodococcus opacus | 1,2-dihydro-3H-indol-3-one + FAD + H2O | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.11 | FAD | - |
Rhodococcus opacus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.14.11 | physiological function | the FAD-to-FAD hydride transfer of the reductase StyB has a rate constant of about 8 per s. This step is rate limiting in the styrene epoxidation reaction and helps to ensure that flavin reduction and styrene epoxidation reactions proceed without wasteful side reactions | Rhodococcus opacus |