文献类型：期刊文献

英文题名：Expression of two old yellow enzyme homologues from Gluconobacter oxydans and identification of their citral hydrogenation abilities

作者：Yin, Bo[1];Yang, Xuepeng[2];Wei, Guodong[1];Ma, Yushu[1];Wei, Dongzhi[1]

机构：[1]E China Univ Sci & Technol, New World Inst Biotechnol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]Zhengzhou Univ Light Ind, Coll Food & Biol Engn, Zhengzhou 450002, Peoples R China

年份：2008

卷号：38

期号：3

起止页码：241

外文期刊名：MOLECULAR BIOTECHNOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000253133600007)】；

语种：英文

外文关键词：Gluconobacter oxydans; old yellow enzyme; citral; NADH FMN-oxidoreductase; citronellal

摘要：Two genes that encode proteins which share 30-35% sequence identity with yeast OYE (Old Yellow Enzyme, an NAD(P)H FMN-oxidoreductase), the well-studied archetype of the OYE protein family, have been identified in Gluconobacter oxydans M5. The two genes are localized in the chromosome and plasmid, respectively. Comparison of the deduced amino acid sequences of the enzymes with database entries revealed 75.1% similarity and 64.9% identity to that of the Pseudomonas syringae pv. glycinea NAD(P)H-dependent 2-cyclohexen-1-one reductase. The two proteins were expressed as His-tag fusion proteins in Escherichia coli and purified. The ability of the purified proteins to hydrogenate citral was identified. The results showed that the alpha,beta-double bond of citral cis-isomer 'neral' could be stereoselectively reduced to produce citronellal by the purified OYE homologues.