CrystalstructureofL-serine3-dehydrogenasecomplexed：丝氨酸脱氢酶复合物的晶体结构.pdfVIP

Photon Factory Activity Report 2013 #31 (2014) B 1A, 5A, NE3A/ 2012G503, 2013G003 + Crystal structure of L-serine 3-dehydrogenase complexed with NAD(P) from Pyrobaculum calidifontis 1 2 1 3 Kazunari Yoneda* , Haruhiko Sakuraba , Tomohiro Araki , Toshihisa Ohshima 1Department of Bioscience, School of Agriculture, Tokai University, Aso, Kumamoto, Japan 2Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, Miki-cho, Kita-gun, Kagawa761-0795, Japan 3 Department of Biomedical Engineering, Osaka Institute of Technology, Osaka, Japan 1 Introduction acid residues 1 to 207, 211 to 283, one NADP+ coemzyme L-Serine dehydrogenase (L-SerDH; EC 1.1.1.276) and 72 waters (Fig. 1, 2). catalyzes the dehydrogenation of L-serine in the presence + of NAD(P) . This enzyme catalyzes dehydrogenation at the -carbon (C3) position of L-serine. The suspected product of the reaction is 2-aminomalonate semialdehyde, which nonenzymatically decomposes into 2- aminoacetaldehyde and CO . 2 Currently, no L-SerDH has been so far reported in archaea, the third domain of life, or in hyperthermophiles. Within the genomic sequence of an aerobic hyperthermophilic archaeon, Pyrobaculum calidifontis, w