1. Identification of Escherichia coli YgaF as an L-2-Hydroxyglutarate Oxidase.
- Author
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Kalliri, Efthalia, Mulrooney, Scott B., and Hausinger, Robert P.
- Subjects
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GENES , *GENETIC regulation , *PROTEINS , *ESCHERICHIA coli , *FLAVINS , *ADENINE , *OXIDASES , *ENZYMES , *PROPIONATES - Abstract
YgaF, a protein of previously unknown function in Escherichia coli, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit L-2-hydroxyglutarate oxidase activity. The inability of anaerobic, reduced enzyme to reverse the reaction by reducing the product α-ketoglutaric acid is explained by the very high reduction potential (+19 mV) of the bound cofactor. The likely role of this enzyme in the cell is to recover α-ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate. On the basis of the identified function, we propose that this gene be renamed lhgO. [ABSTRACT FROM AUTHOR]
- Published
- 2008
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