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Literature summary for 1.14.14.11 extracted from

  • Tischler, D.; Schloemann, M.; van Berkel, W.J.; Gassner, G.T.
    FAD C(4a)-hydroxide stabilized in a naturally fused styrene monooxygenase (2013), FEBS Lett., 587, 3848-3852.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 pLysS cells Rhodococcus opacus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
styrene + FADH2 + O2 Rhodococcus opacus
-
styrene oxide + FAD + H2O
-
?
styrene + FADH2 + O2 Rhodococcus opacus 1CP
-
styrene oxide + FAD + H2O
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus opacus
-
-
-
Rhodococcus opacus 1CP
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA affinity column chromatography Rhodococcus opacus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
styrene + FADH2 + O2
-
Rhodococcus opacus styrene oxide + FAD + H2O
-
?
styrene + FADH2 + O2
-
Rhodococcus opacus 1CP styrene oxide + FAD + H2O
-
?

Synonyms

Synonyms Comment Organism
StyA2B
-
Rhodococcus opacus
StyAB
-
Rhodococcus opacus

Cofactor

Cofactor Comment Organism Structure
FADH2
-
Rhodococcus opacus