PMID:18390652
| Citation |
Kalliri, E, Mulrooney, SB and Hausinger, RP (2008) Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase. J. Bacteriol. 190:3793-8 |
|---|---|
| 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. |
| Links |
PubMed PMC2395033 Online version:10.1128/JB.01977-07 |
| Keywords |
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 |
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This paper describes the purification of YgaF from a clone.
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