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Literature summary for 1.14.14.11 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.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
NaCl a salt concentration of 162 mM results in half of the maximum inhibitory effect Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
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Synonyms

Synonyms Comment Organism
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
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

Cofactor Comment Organism Structure
FADH2 NSMOA binds tightly to reduced FAD. FAD C(4a)-peroxide is the oxygen atom donor Pseudomonas putida