Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase |
| |
Authors: | Bowater Laura Fairhurst Shirley A Just Victoria J Bornemann Stephen |
| |
Institution: | Biological Chemistry Department, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|