Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase

J Bacteriol. 2008 Jun;190(11):3793-8. doi: 10.1128/JB.01977-07. Epub 2008 Apr 4.


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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / genetics
  • Alcohol Oxidoreductases / metabolism*
  • Cloning, Molecular
  • Escherichia coli K12 / genetics
  • Escherichia coli K12 / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Gene Expression Regulation, Bacterial
  • Glutarates / chemistry
  • Glutarates / metabolism


  • Escherichia coli Proteins
  • Glutarates
  • alpha-hydroxyglutarate
  • Alcohol Oxidoreductases
  • 2-hydroxyglutarate dehydrogenase