鉴定大肠杆菌YgaF为L-2-羟基戊二酸氧化酶。
Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase.
作者信息
Kalliri Efthalia, Mulrooney Scott B, Hausinger Robert P
机构信息
6193 Biomedical Physical Sciences, Michigan State University, East Lansing, MI 48824-4320, USA.
出版信息
J Bacteriol. 2008 Jun;190(11):3793-8. doi: 10.1128/JB.01977-07. Epub 2008 Apr 4.
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.
摘要
YgaF是一种在大肠杆菌中功能未知的蛋白质，已证明它含有非共价结合的黄素腺嘌呤二核苷酸，并具有L-2-羟基戊二酸氧化酶活性。厌氧状态下还原态的酶无法通过还原产物α-酮戊二酸来逆转反应，这是由于结合辅因子的还原电位非常高（+19 mV）。该酶在细胞中的可能作用是回收被其他酶错误还原或在以丙酸盐为碳源生长过程中形成的α-酮戊二酸。基于已确定的功能，我们建议将该基因重新命名为lhgO。
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