Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase.
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.
Bowater
Laura
L
Biological Chemistry Department, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.
Fairhurst
Shirley A
SA
Just
Victoria J
VJ
Bornemann
Stephen
S
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D017124:Conserved Sequence; D049308:Dioxygenases; D004578:Electron Spin Resonance Spectroscopy; D006801:Humans; D007501:Iron / Q000032:analysis; D008969:Molecular Sequence Data; D010105:Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013053:Spectrophotometry
D007501:Iron; D010105:Oxygenases; D049308:Dioxygenases; C003281:quercetin 2,3-dioxygenase