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Literature summary for 1.14.13.69 extracted from

  • Gallagher, S.C.; Cammack, R.; Dalton, H.
    Electron transfer reactions in the alkene mono-oxygenase complex from Nocardia corallina B-276 (1999), Biochem. J., 339, 79-85.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation Gordonia rubripertincta
[2Fe-2S]cluster the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation Gordonia rubripertincta

Organism

Organism UniProt Comment Textmining
Gordonia rubripertincta
-
multi-component enzyme
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Gordonia rubripertincta
-
B-276
-
Gordonia rubripertincta B-276
-
B-276
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
propene + NADH + H+ + O2
-
Gordonia rubripertincta 1,2-epoxypropane + NAD+ + H2O
-
?
propene + NADH + H+ + O2
-
Gordonia rubripertincta B-276 1,2-epoxypropane + NAD+ + H2O
-
?

Subunits

Subunits Comment Organism
More multi-component enzyme Gordonia rubripertincta

Cofactor

Cofactor Comment Organism Structure
FAD the reductase component contains two prosthetic groups, an FAD centre and a [2Fe-2S] cluster. The FAD moiety is reduced by bound NADH in a two-electron reaction. The electrons are then transported to the [2Fe-2S] centre one at a time, which reduces the di-iron centre of the epoxydase. Reduction of the di-iron centre is required for oxygen binding and substrate oxidation Gordonia rubripertincta