Literature summary extracted from
Kantz, A.; Gassner, G.T.
Nature of the reaction intermediates in the flavin adenine dinucleotide-dependent epoxidation mechanism of styrene monooxygenase (2010), Biochemistry, 50, 523-532.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.14.14.11 |
NaCl |
a salt concentration of 162 mM results in half of the maximum inhibitory effect |
Pseudomonas putida |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.14.14.11 |
Pseudomonas putida |
- |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.14.14.11 |
styrene + FADH2 + O2 |
mechanism: molecular oxygen first reacts with NSMOA(FADred) to yield an FAD C(4a)-peroxide intermediate. This species is nonfluorescent and has an absorbance maximum of 382 nm. Styrene then reacts with the peroxide intermediate to yield a fluorescent intermediate (FAD C(4a)-hydroxide) with an absorbance maximum of 368 nm |
Pseudomonas putida |
(S)-2-phenyloxirane + FAD + H2O |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.14.14.11 |
NSMOA |
styrene monooxygenase (SMO) is a two-component flavoenzyme composed of an NADH-specific flavin reductase (SMOB) and FAD-specific styrene epoxidase (NSMOA) |
Pseudomonas putida |
1.14.14.11 |
SMO |
styrene monooxygenase (SMO) is a two-component flavoenzyme composed of an NADH-specific flavin reductase (SMOB) and FAD-specific styrene epoxidase (NSMOA) |
Pseudomonas putida |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.14.14.11 |
FADH2 |
NSMOA binds tightly to reduced FAD. FAD C(4a)-peroxide is the oxygen atom donor |
Pseudomonas putida |
|