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

Bowater, Laura, Fairhurst, Shirley A, Just, Victoria J and Bornemann, Stephen (2004) Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase. FEBS Letters, 557 (1-3). pp. 45-48. ISSN 1873-3468

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Abstract

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.

Item Type:	Article
Faculty \ School:	Faculty of Medicine and Health Sciences > Norwich Medical School Faculty of Science > School of Biological Sciences Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009)
Depositing User:	Rhiannon Harvey
Date Deposited:	31 May 2011 12:02
Last Modified:	02 Mar 2023 17:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/31576
DOI:	10.1016/S0014-5793(03)01439-X

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