characterization of an archaeal malic enzyme from the hyperthermophilic archaeon thermococcus kodakaraensis kod1特征的古细菌的苹果酸脱氢酶hyperthermophilic archaeon thermococcus kodakaraensis kod1.pdfVIP

Archaea 1, 293–301 © 2005 Heron Publishing—Victoria, Canada Characterization of an archaeal malic enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 1 1 1,2 1 WAKAO FUKUDA, YULIA SARI ISMAIL, TOSHIAKI FUKUI, HARUYUKI ATOMI and 1,3 TADAYUKI IMANAKA 1 Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura,Nishikyo-ku, Kyoto 615-8510, Japan 2 Present address: Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259Nagatsuta, Midori-ku, Yokohama 226-8501, Japan 3 Corresponding author (imanaka@sbchem.kyoto-u.ac.jp) Received September 9, 2004; accepted December 16, 2004; published online January 6, 2005 Summary Although the interconversion between C4 and C3 metabolites is important in maintaining the levels of interme- compounds has an important role in overall metabolism, lim- diates in the tricarboxylic acid (TCA) cycle. When TCA cycle ited information is available on the properties and regulation of metabolites are consumed, OAA can be replenished from PEP enzymes acting on these metabolites in hyperthermophilic or pyruvate, or both. When these metabolites are in excess, this archaea. Malic enzyme is one of the enzymes involved in this link can be utilized in the opposite direction to remove and di- interconversion, catalyzing the oxidative decarboxylation of rect the carbon flux toward other pathways such as gluconeo- malate to pyruvate as well as the reductive carboxylation cou- genesis (Owen et al. 2002). The enzymes catalyzi