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Bacillus subtilis YxaG is a novel Fe‐containing quercetin 2,3‐dioxygenase
Author(s) -
Bowater Laura,
Fairhurst Shirley A,
Just Victoria J,
Bornemann Stephen
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01439-x
Subject(s) - bacillus subtilis , dioxygenase , enzyme , chemistry , cofactor , oxalate , carbon monoxide , biochemistry , stereochemistry , biology , bacteria , catalysis , genetics , inorganic chemistry
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 .