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
Full text not available from this repository. (Request a copy)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 |
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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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