Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase
Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase
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DOI：
10.1128/jb.01977-07
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发表时间：
2008-06-01
影响因子：
3.2
通讯作者：
Hausinger, Robert P.
中科院分区：
文献类型：
--
作者：
Kalliri, Efthalia;Mulrooney, Scott B.;Hausinger, Robert P.
YgaF 是一种在大肠杆菌中功能未知的蛋白质，已被证明具有非共价结合的黄素腺嘌呤二核苷酸并表现出 L-2-羟基戊二酸氧化酶活性。厌氧还原酶无法通过还原产物 α-酮戊二酸来逆转反应，这是因为结合的辅因子具有非常高的还原电位（+19 mV）。这种酶在细胞中的可能作用是回收被其他酶错误还原或在丙酸盐生长过程中形成的α-酮戊二酸。根据已确定的功能，我们建议将该基因更名为lhgO。
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.