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

被引：29

作者：

Kalliri, Efthalia ^{[2
]}

Mulrooney, Scott B. ^{[1
]}

Hausinger, Robert P. ^{[1
,3
]}

机构：

[1] Michigan State Univ, Dept Microbiol & Mol Genet, E Lansing, MI 48824 USA

[2] Michigan State Univ, Dept Chem, E Lansing, MI 48824 USA

[3] Michigan State Univ, Dept Biochem & Mol Biol, E Lansing, MI 48824 USA

来源：

JOURNAL OF BACTERIOLOGY | 2008年 / 190卷 / 11期

关键词：

D O I：

10.1128/JB.01977-07

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：3793 / 3798

页数：6

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