Contains FAD. This enzyme, characterized from the bacterium Pseudomonas sp. SG-MS2, catalyses the incorporation of an oxygen atom originating from a water molecule into position C-6 of the lignan (+)-pinoresinol. The enzyme consists of a flavoprotein subunit and a c-type cytochrome subunit. Electrons that originate in the substrate are transferred via the FAD cofactor and the cytochrome subunit to the blue-copper protein azurin.
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The expected taxonomic range for this enzyme is: Pseudomonas sp. SG-MS2
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SYSTEMATIC NAME
IUBMB Comments
(+)-pinoresinol:azurin oxidoreductase
Contains FAD. This enzyme, characterized from the bacterium Pseudomonas sp. SG-MS2, catalyses the incorporation of an oxygen atom originating from a water molecule into position C-6 of the lignan (+)-pinoresinol. The enzyme consists of a flavoprotein subunit and a c-type cytochrome subunit. Electrons that originate in the substrate are transferred via the FAD cofactor and the cytochrome subunit to the blue-copper protein azurin.
the pinoresinol-oxidizing enzyme in Pseudomonas sp. SG-MS2 is a flavocytochrome complex produced by the translationally coupled BLX42_10690 and BLX42_10695 genes
Shettigar, M.; Balotra, S.; Kasprzak, A.; Pearce, S.L.; Lacey, M.J.; Taylor, M.C.; Liu, J.W.; Cahill, D.; Oakeshott, J.G.; Pandey, G.
Oxidative catabolism of (+)-pinoresinol is initiated by an unusual flavocytochrome encoded by translationally coupled genes within a cluster of (+)-pinoresinol-coinduced genes in Pseudomonas sp. strain SG-MS2