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Journal of Bacteriology, June 2008, p. 3793-3798, Vol. 190, No. 11
0021-9193/08/$08.00+0     doi:10.1128/JB.01977-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Identification of Escherichia coli YgaF as an L-2-Hydroxyglutarate Oxidase{triangledown}

Efthalia Kalliri,1 Scott B. Mulrooney,2 and Robert P. Hausinger2,3*

Department of Chemistry,1 Department of Microbiology and Molecular Genetics,2 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 488243

Received 20 December 2007/ Accepted 18 March 2008

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 {alpha}-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 {alpha}-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.

* Corresponding author. Mailing address: 6193 Biomedical Physical Sciences, Michigan State University, East Lansing, MI 48824-4320. Phone: (517) 355-6463, ext. 1610. Fax: (517) 355-8957. E-mail: hausinge{at}msu.edu

{triangledown} Published ahead of print on 4 April 2008.

Journal of Bacteriology, June 2008, p. 3793-3798, Vol. 190, No. 11
0021-9193/08/$08.00+0     doi:10.1128/JB.01977-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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