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FEBS Lett. 2004 Jan 16;557(1-3):45-8.

Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase.

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Biological Chemistry Department, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.


The Bacillus subtilis genome contains genes for three hypothetical proteins belonging to the bicupin family, two of which we have previously shown to be Mn(II)-dependent oxalate decarboxylases. We have now shown that the third, YxaG, exhibits quercetin 2,3-dioxygenase activity and that it contains Fe ions. This contrasts with the eukaryotic enzyme which contains a Cu ion. YxaG is the first prokaryotic carbon monoxide-forming enzyme that utilises a flavonol to be characterised and is only the second example of a prokaryotic dioxygenolytic carbon monoxide-forming enzyme known to contain a cofactor. It is proposed to rename the B. subtilis gene qdoI.

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