naa a22 4500 51081977X CHVBK 20180411083525.0 cr unu---uuuuu 180411e20130701xx s 000 0 eng 10.1007/s11814-013-0061-4 doi (NATIONALLICENCE)springer-10.1007/s11814-013-0061-4 Expression characteristics of the maeA and maeB genes by extracellular malate and pyruvate in Escherichia coli [Elektronische Daten] [Irisappan Ganesh, Sambandam Ravikumar, Si Park, Seung Lee, Soon Hong] The malate-pyruvate conversion pathway is catalyzed by two malic enzyme isomers, MaeA and MaeB. qRT-PCR was carried out under malate and pyruvate supplemented conditions to understand the dynamics of maeA and maeB gene expression. maeA expression was elevated by malate, and maeB expression was inhibited by levels of both malate and pyruvate higher than 0.1 mM. Green fluorescent protein (GFP) reporter plasmids were also constructed by integration of the maeA/maeB promoter with the gfp gene. We showed that maeA driven GFP expression was positively and negatively correlated with extracellular malate and pyruvate induction. In contrast, no significant changes in maeB driven GFP expression were observed under both malate and pyruvate supplemented conditions. Korean Institute of Chemical Engineers, Seoul, Korea, 2013 Malate nationallicence Pyruvate nationallicence maeA nationallicence maeB nationallicence Green Fluorescent Protein nationallicence Escherichia coli nationallicence Ganesh Irisappan Department of Chemical Engineering, University of Ulsan, 93 Daehak-ro, Nam-gu, 680-749, Ulsan, Korea aut Ravikumar Sambandam Department of Pharmaceutical Science and Technology, Catholic University of Daegu, 330, Geumrak 1-ri, Hayang-eup, Gyeongsan-si, 712-702, Gyeongbuk, Korea aut Park Si Department of Environmental Engineering and Energy, Myongji University, San 38-2, Nam-dong, Cheoin-gu, Yongin-si, 449-728, Gyeonggido, Korea aut Lee Seung Chemical Biotechnology Research Center, Korea Research Institute of Chemical Technology, 305-600, Yuseong-gu, Daejeon, Korea aut Hong Soon Department of Chemical Engineering, University of Ulsan, 93 Daehak-ro, Nam-gu, 680-749, Ulsan, Korea aut Korean Journal of Chemical Engineering Springer US; http://www.springer-ny.com 30/7(2013-07-01), 1443-1447 0256-1115 30:7<1443 2013 30 11814 https://doi.org/10.1007/s11814-013-0061-4 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11814-013-0061-4 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ganesh Irisappan Department of Chemical Engineering, University of Ulsan, 93 Daehak-ro, Nam-gu, 680-749, Ulsan, Korea aut NATIONALLICENCE 700 1- Ravikumar Sambandam Department of Pharmaceutical Science and Technology, Catholic University of Daegu, 330, Geumrak 1-ri, Hayang-eup, Gyeongsan-si, 712-702, Gyeongbuk, Korea aut NATIONALLICENCE 700 1- Park Si Department of Environmental Engineering and Energy, Myongji University, San 38-2, Nam-dong, Cheoin-gu, Yongin-si, 449-728, Gyeonggido, Korea aut NATIONALLICENCE 700 1- Lee Seung Chemical Biotechnology Research Center, Korea Research Institute of Chemical Technology, 305-600, Yuseong-gu, Daejeon, Korea aut NATIONALLICENCE 700 1- Hong Soon Department of Chemical Engineering, University of Ulsan, 93 Daehak-ro, Nam-gu, 680-749, Ulsan, Korea aut NATIONALLICENCE 773 0- Korean Journal of Chemical Engineering Springer US; http://www.springer-ny.com 30/7(2013-07-01), 1443-1447 0256-1115 30:7<1443 2013 30 11814 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer