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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

<jats:p>The <jats:italic>Bacillus subtilis</jats:italic> 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 <jats:italic>B. subtilis</jats:italic> gene <jats:italic>qdoI</jats:italic>.</jats:p>
Original languageEnglish
Pages (from-to)45-48
Number of pages0
JournalFEBS Letters
Volume557
Issue number0
Early online date13 Dec 2003
DOIs
Publication statusPublished - 16 Jan 2004

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