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J. Bacteriol. doi:10.1128/JB.01977-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Identification of Escherichia coli YgaF as L-2-Hydroxyglutarate Oxidase

Department of Chemistry, Department of Microbiology and Molecular Genetics, and Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824

^* To whom correspondence should be addressed. Email: hausinge{at}msu.edu.

	Abstract

YgaF, a protein of previously unknown function in Escherichia coli, was shown to possess non-covalently bound FAD and to exhibit L-2-hydroxyglutarate oxidase activity. The inability of anaerobic, reduced enzyme to reverse the reaction by reducing the product -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 -ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate. On the basis of the identified function, we propose to rename this gene lhgO.