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Masafumi Hidaka is a postdoctoral fellow in the Laboratory of Enzymology at Department of Biotechnology, The University of Tokyo. He received his Ph.D. from the Graduate School of Agricultural and Life Sciences, The University of Tokyo in 2005, under the supervision of Prof. Hirofumi Shoun. He joined the group of Dr. Motomitsu Kitaoka as a Japan Society for the Promotion of Science Research fellow (2005-2008). Subsequently, he moved to the University of Tokyo to join the group of Dr. Shinya Fushinobu. His research interests are the structural insights into mechanism of enzymatic reaction. He has determined the crystal structures of
- GH8 reducing-end-xylose releasing exo-oligoxylanase 
- GH42 β-galactosidase 
- GH94 chitobiose phosphorylase  and cellobiose phosphorylase 
- GH112 β-1,3-D-galactosyl-D-hexososamine phosphorylase 
- Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, and Kitaoka M. (2005). Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125. J Biol Chem. 2005;280(17):17180-6. DOI:10.1074/jbc.M413693200 |
- Hidaka M, Fushinobu S, Ohtsu N, Motoshima H, Matsuzawa H, Shoun H, and Wakagi T. (2002). Trimeric crystal structure of the glycoside hydrolase family 42 beta-galactosidase from Thermus thermophilus A4 and the structure of its complex with galactose. J Mol Biol. 2002;322(1):79-91. DOI:10.1016/s0022-2836(02)00746-5 |
- Hidaka M, Honda Y, Kitaoka M, Nirasawa S, Hayashi K, Wakagi T, Shoun H, and Fushinobu S. (2004). Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (alpha/alpha)(6) barrel fold. Structure. 2004;12(6):937-47. DOI:10.1016/j.str.2004.03.027 |
- Hidaka M, Kitaoka M, Hayashi K, Wakagi T, Shoun H, and Fushinobu S. (2006). Structural dissection of the reaction mechanism of cellobiose phosphorylase. Biochem J. 2006;398(1):37-43. DOI:10.1042/BJ20060274 |
- Hidaka M, Nishimoto M, Kitaoka M, Wakagi T, Shoun H, and Fushinobu S. (2009). The crystal structure of galacto-N-biose/lacto-N-biose I phosphorylase: a large deformation of a TIM barrel scaffold. J Biol Chem. 2009;284(11):7273-83. DOI:10.1074/jbc.M808525200 |