期刊
JOURNAL OF BACTERIOLOGY
卷 190, 期 11, 页码 3793-3798出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.01977-07
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- NIGMS NIH HHS [R01 GM063584, GM065384] Funding Source: Medline
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.
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