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

Laura Bowater, Shirley A Fairhurst, Victoria J Just, Stephen Bornemann

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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.
Original languageEnglish
Pages (from-to)45-48
Number of pages4
JournalFEBS Letters
Issue number1-3
Publication statusPublished - 2004

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