Related Experiment Video
Updated: Jul 6, 2026

Characterization of a Pathogenic Escherichia coli Strain Derived from Oreochromis spp. Farms Using Whole-Genome Sequencing
Published on: December 23, 2022
Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase
Efthalia Kalliri1, Scott B Mulrooney, Robert P Hausinger
16193 Biomedical Physical Sciences, Michigan State University, East Lansing, MI 48824-4320, USA.
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 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.
Related Concept Videos
Stringent Response in E. coli
Bacterial Gastroenteritis
DNA Agarose Gel Electrophoresis
Gel extraction follows five major steps: running gel electrophoresis to separate fragments, isolating the individual bands, extracting DNA from those bands, and removing the dye and salts from the extracted mixture to obtain pure DNA.
In cloning experiments, both the insert and vector DNA...
Chemotaxis in E. coli

