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 F...

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Bibliographic Details
Published in:FEBS letters 2004-01, Vol.557 (1), p.45-48
Main Authors: Bowater, Laura, Fairhurst, Shirley A, Just, Victoria J, Bornemann, Stephen
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacillus subtilis
Bacillus subtilis - enzymology
Bacillus subtilis - genetics
Carbon monoxide production
Conserved Sequence
Dioxygenases
Electron Spin Resonance Spectroscopy
Flavonol
Humans
Iron
Iron - analysis
MALDI-TOF, matrix-assisted laser desorption/ionisation time of flight
Molecular Sequence Data
Oxygenases - chemistry
Oxygenases - genetics
Oxygenases - metabolism
PAGE, polyacrylamide gel electrophoresis
PCR, polymerase chain reaction
Prokaryote
Quercetin 2,3-dioxygenase
Sequence Alignment
Sequence Homology, Amino Acid
Spectrophotometry
Tris, tris(hydroxymethyl)aminomethane
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(03)01439-X