Cloned (Comment) | Organism |
---|---|
functional expression of His10-StyA2B in Escherichia coli | Rhodococcus opacus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
44000 | - |
2 * 44000, SDS-PAGE | Rhodococcus opacus |
80000 | - |
gel filtration | Rhodococcus opacus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
styrene + FADH2 + O2 | Rhodococcus opacus | - |
(S)-2-phenyloxirane + FAD + H2O | - |
? | |
styrene + FADH2 + O2 | Rhodococcus opacus 1CP | - |
(S)-2-phenyloxirane + FAD + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rhodococcus opacus | C7ACG0 | StyA1 | - |
Rhodococcus opacus 1CP | C7ACG0 | StyA1 | - |
Purification (Comment) | Organism |
---|---|
- |
Rhodococcus opacus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-chlorostyrene + FADH2 + O2 | - |
Rhodococcus opacus | (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O | - |
? | |
2-chlorostyrene + FADH2 + O2 | - |
Rhodococcus opacus 1CP | (2S)-2-(2-chlorophenyl)oxirane + FAD + H2O | - |
? | |
3-chlorostyrene + FADH2 + O2 | - |
Rhodococcus opacus | (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O | - |
? | |
3-chlorostyrene + FADH2 + O2 | - |
Rhodococcus opacus 1CP | (2S)-2-(3-chlorophenyl)oxirane + FAD + H2O | - |
? | |
4-chlorostyrene + FADH2 + O2 | - |
Rhodococcus opacus | (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O | - |
? | |
4-chlorostyrene + FADH2 + O2 | - |
Rhodococcus opacus 1CP | (2S)-2-(4-chlorophenyl)oxirane + FAD + H2O | - |
? | |
4-methylstyrene + FADH2 + O2 | - |
Rhodococcus opacus | ? + FAD + H2O | - |
? | |
styrene + FADH2 + O2 | - |
Rhodococcus opacus | (S)-2-phenyloxirane + FAD + H2O | - |
? | |
styrene + FADH2 + O2 | StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity | Rhodococcus opacus | (S)-2-phenyloxirane + FAD + H2O | - |
? | |
styrene + FADH2 + O2 | - |
Rhodococcus opacus 1CP | (S)-2-phenyloxirane + FAD + H2O | - |
? | |
styrene + FADH2 + O2 | StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity | Rhodococcus opacus 1CP | (S)-2-phenyloxirane + FAD + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 44000, SDS-PAGE | Rhodococcus opacus |
Synonyms | Comment | Organism |
---|---|---|
StyA1 | - |
Rhodococcus opacus |
StyA1/StyA2B | StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity | Rhodococcus opacus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FADH2 | StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity | Rhodococcus opacus |