文献类型：期刊文献

英文题名：Enhanced aldehyde dehydrogenase activity by regenerating NAD+ in Klebsiella pneumoniae and implications for the glycerol dissimilation pathways

作者：Li, Ying[1]; Su, Mingyue[1]; Ge, Xizhen[2]; Tian, Pingfang[1]

第一作者：Li, Ying

通讯作者：Tian, P.

机构：[1] College of Life Science and Technology, Beijing University of Chemical Technology, 100029 Beijing, China; [2] College of Biochemical Engineering, Beijing Union University, 100023 Beijing, China

第一机构：College of Life Science and Technology, Beijing University of Chemical Technology, 100029 Beijing, China

通讯机构：[1]College of Life Science and Technology, Beijing University of Chemical Technology, 100029 Beijing, China

年份：2013

卷号：35

期号：10

起止页码：1609-1615

外文期刊名：Biotechnology Letters

收录：EI(收录号：20134016815842);Scopus(收录号：2-s2.0-84884818621)

语种：英文

外文关键词：Yeast - Bacteria - Cell proliferation - Aldehydes

摘要：In Klebsiella pneumoniae, 3-hydroxypropaldehyde is converted to 3-hydroxypropionic acid (3-HP) by aldehyde dehydrogenase (ALDH) with NAD+ as a cofactor. Although ALDH overexpression stimulates the formation of 3-HP, it ceases to accumulate when NAD+ is exhausted. Here we show that NAD+ regeneration, together with ALDH overexpression, facilitates 3-HP production and benefits cell growth. Three distinct NAD+-regenerating enzymes: NADH oxidase and NADH dehydrogenase from K. pneumoniae, and glycerol-3-phosphate dehydrogenase (GPD1) from Saccharomyces cerevisiae, were individually expressed in K. pneumoniae. In vitro assay showed their higher activities than that of the control, indicating their capacities to regenerate NAD+. When they were respectively co-expressed with ALD4, an ALDH from S. cerevisiae, the activities of ALD4 were significantly elevated compared with that expressing ALD4 alone, suggesting that the regenerated NAD+ enhanced the activity of ALD4. More interestingly, the growth rates of all NAD+-regenerating strains were prolonged in comparison with the control, indicating that NAD+ regeneration stimulated cell proliferation. This study not only reveals the reliance of ALD4 activity on NAD+ availability but also provides a method for regulating the dha regulon. ? 2013 Springer Science+Business Media Dordrecht.