Characterization of H2O-forming NADH oxidase from Streptococcus pyogenes and its application in L-rare sugar production

被引:44
作者
Gao, Hui [1 ]
Tiwari, Manish Kumar [1 ]
Kang, Yun Chan [1 ]
Lee, Jung-Kul [1 ,2 ]
机构
[1] Konkuk Univ, Dept Chem Engn, Seoul 143701, South Korea
[2] Konkuk Univ, Inst SK KU Biomat, Seoul 143701, South Korea
基金
新加坡国家研究基金会;
关键词
Cofactor regeneration; H2O-forming NADH oxidase; L-Rare sugar; Streptococcus pyogenes; FLAVOPROTEIN DISULFIDE REDUCTASES; GLUTATHIONE-REDUCTASE; BACILLUS-PALLIDUS; PURIFICATION; CONVERSION; CATALYSIS; COFACTOR; FAECALIS; CLONING; ENZYME;
D O I
10.1016/j.bmcl.2012.01.049
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
A nicotinamide adenine dinucleotide (NADH) oxidase from Streptococcus pyogenes MGAS10394 (SpNox) was cloned and overexpressed in Escherichia coli BL21 (DE3). The purified SpNox enzyme had optimal pH and temperature of 7.0 and 55 degrees C, respectively, with a K-m of 27.0 mu M and a k(cat)/K-m of 1.1 x 10(7) s (1) M (1). SpNox showed the highest activity among all known NADH oxidases, and site-directed mutagenesis and docking analysis shed light on the molecular basis of its unusually high activity. The characteristics of SpNox may prove to be useful for NAD(+) regeneration in the production of L-rare sugar. (c) 2012 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1931 / 1935
页数:5
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