EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.14.14.11 | the crystal structure of the N-terminally histidine-tagged epoxidase component of this system, NSMOA, determined to 2.3 A resolution, indicates the enzyme exists as a homodimer in which each monomer forms two distinct domains | Pseudomonas putida |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.11 | styrene + FADH2 + O2 | Pseudomonas putida | - |
(S)-2-phenyloxirane + FAD + H2O | - |
? | |
1.14.14.11 | styrene + FADH2 + O2 | Pseudomonas putida S12 | - |
(S)-2-phenyloxirane + FAD + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.11 | Pseudomonas putida | O33471 | - |
- |
1.14.14.11 | Pseudomonas putida S12 | O33471 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.14.11 | N-terminally histidine-tagged styrene monooxygenase | Pseudomonas putida |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.11 | styrene + FADH2 + O2 | - |
Pseudomonas putida | (S)-2-phenyloxirane + FAD + H2O | - |
? | |
1.14.14.11 | styrene + FADH2 + O2 | preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene | Pseudomonas putida | (S)-2-phenyloxirane + FAD + H2O | - |
? | |
1.14.14.11 | styrene + FADH2 + O2 | - |
Pseudomonas putida S12 | (S)-2-phenyloxirane + FAD + H2O | - |
? | |
1.14.14.11 | styrene + FADH2 + O2 | preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene | Pseudomonas putida S12 | (S)-2-phenyloxirane + FAD + H2O | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.14.11 | homodimer | each monomer forms two distinct domains | Pseudomonas putida |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.14.11 | NSMOA | - |
Pseudomonas putida |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.11 | FADH2 | flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA about 8000times more tightly than the oxidized coenzyme | Pseudomonas putida |