User:Masahiro Nakajima

Masahiro Nakajima received his Ph.D. from the Graduate School of Agricultural and Life Science, The University of Tokyo in 2006. He joined the group of Dr. Motomitsu Kitaoka as a postdoctoral fellow (2006–2010). He moved to Iwate Biotechnology Research Center as a researcher (2010–2012). He was an assistant professor in Taguchi Laboratory (2012–2020) and is currently an associate professor in his own laboratory (2020-) at Department of Applied Biological Science, Tokyo University of Science. His research currently focuses on structures and functions of carbohydrate-active enzymes acting on unique sugar chains such as β-1,2-glucan. He acts as a Responsible Curator of Glycoside Hydrolase Families GH144, GH162, GH186, GH189, GH192, GH193 and GH194, and also created clan GH-S. He determined the functions and/or crystal structures of

• GH1 β-Glucosidase [1]

• GH3 β-Glucosidases [2, 3, 4]
• GH16 β-1,3-Glucanase [5]
• GH35 β-1,2-Glucosyltransglycosylase [6] (new EC number) and β-1,2-galactosidase [7] (new EC number enzyme)
• GH38 α-Mannosidase [8]
• GH57 4-α-Glucanotransferase [9]
• GH94 1,2-β-Oligoglucan phosphorylases [10, 11] (new EC number)
• GH112 D-Galactosyl-β-1,4-L-rhamnose phosphorylase [12] (new EC number) and β-1,3-galactosyl-N-acetylhexosamine phosphorylases [12, 13, 14, 15]
• GH144 Bacterial β-1,2-glucanases [16] (family created) and sophorosylhydrolase [17] (new EC number)
• GH162 Fungal β-1,2-glucanase [18] (family created) (clan GH-S created)
• GH186 E. coli β-1,2-glucanase [19] (family created) and α-1,6-cyclized β-1,2-glucohexadecaose synthase from Xanthomonas campestris pv. campestris (new EC number enzyme)[20]
• GH189 Cyclic β-1,2-glucan synthase (transglycosylase domain) [21] (family created) (new EC number)
• GH192 Bacterial β-1,2-glucanase [22] (family created)
• GH193 Bacterial β-1,2-glucanase [22] (family created)
• GH194 Bacterial β-1,2-glucanase [22] (family created)

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2. Nakajima M, Yamashita T, Takahashi M, Nakano Y, and Takeda T. (2012). Identification, cloning, and characterization of β-glucosidase from Ustilago esculenta. Appl Microbiol Biotechnol. 2012;93(5):1989-98. DOI:10.1007/s00253-011-3538-2 |
3. Nakajima M, Yoshida R, Miyanaga A, Abe K, Takahashi Y, Sugimoto N, Toyoizumi H, Nakai H, Kitaoka M, and Taguchi H. (2016). Functional and Structural Analysis of a β-Glucosidase Involved in β-1,2-Glucan Metabolism in Listeria innocua. PLoS One. 2016;11(2):e0148870. DOI:10.1371/journal.pone.0148870 |
4. Ishiguro R, Tanaka N, Abe K, Nakajima M, Maeda T, Miyanaga A, Takahashi Y, Sugimoto N, Nakai H, and Taguchi H. (2017). Function and structure relationships of a β-1,2-glucooligosaccharide-degrading β-glucosidase. FEBS Lett. 2017;591(23):3926-3936. DOI:10.1002/1873-3468.12911 |
5. Nakajima M, Yamashita T, Takahashi M, Nakano Y, and Takeda T. (2012). A novel glycosylphosphatidylinositol-anchored glycoside hydrolase from Ustilago esculenta functions in β-1,3-glucan degradation. Appl Environ Microbiol. 2012;78(16):5682-9. DOI:10.1128/AEM.00483-12 |
8. Nakajima M, Imamura H, Shoun H, and Wakagi T. (2003). Unique metal dependency of cytosolic alpha-mannosidase from Thermotoga maritima, a hyperthermophilic bacterium. Arch Biochem Biophys. 2003;415(1):87-93. DOI:10.1016/s0003-9861(03)00222-4 |
9. Nakajima M, Imamura H, Shoun H, Horinouchi S, and Wakagi T. (2004). Transglycosylation activity of Dictyoglomus thermophilum amylase A. Biosci Biotechnol Biochem. 2004;68(11):2369-73. DOI:10.1271/bbb.68.2369 |
10. Nakajima M, Tanaka N, Furukawa N, Nihira T, Kodutsumi Y, Takahashi Y, Sugimoto N, Miyanaga A, Fushinobu S, Taguchi H, and Nakai H. (2017). Mechanistic insight into the substrate specificity of 1,2-β-oligoglucan phosphorylase from Lachnoclostridium phytofermentans. Sci Rep. 2017;7:42671. DOI:10.1038/srep42671 |
11. Nakajima M, Toyoizumi H, Abe K, Nakai H, Taguchi H, and Kitaoka M. (2014). 1,2-β-Oligoglucan phosphorylase from Listeria innocua. PLoS One. 2014;9(3):e92353. DOI:10.1371/journal.pone.0092353 |
12. Nakajima M, Nishimoto M, and Kitaoka M. (2009). Characterization of three beta-galactoside phosphorylases from Clostridium phytofermentans: discovery of d-galactosyl-beta1->4-l-rhamnose phosphorylase. J Biol Chem. 2009;284(29):19220-7. DOI:10.1074/jbc.M109.007666 |
13. Nakajima M, Nishimoto M, and Kitaoka M. (2009). Characterization of beta-1,3-galactosyl-N-acetylhexosamine phosphorylase from Propionibacterium acnes. Appl Microbiol Biotechnol. 2009;83(1):109-15. DOI:10.1007/s00253-008-1838-y |
14. Nakajima M and Kitaoka M. (2008). Identification of lacto-N-Biose I phosphorylase from Vibrio vulnificus CMCP6. Appl Environ Microbiol. 2008;74(20):6333-7. DOI:10.1128/AEM.02846-07 |
15. Nakajima M, Nihira T, Nishimoto M, and Kitaoka M. (2008). Identification of galacto-N-biose phosphorylase from Clostridium perfringens ATCC13124. Appl Microbiol Biotechnol. 2008;78(3):465-71. DOI:10.1007/s00253-007-1319-8 |
16. Abe K, Nakajima M, Yamashita T, Matsunaga H, Kamisuki S, Nihira T, Takahashi Y, Sugimoto N, Miyanaga A, Nakai H, Arakawa T, Fushinobu S, and Taguchi H. (2017). Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family. J Biol Chem. 2017;292(18):7487-7506. DOI:10.1074/jbc.M116.762724 |
17. Shimizu H, Nakajima M, Miyanaga A, Takahashi Y, Tanaka N, Kobayashi K, Sugimoto N, Nakai H, and Taguchi H. (2018). Characterization and Structural Analysis of a Novel exo-Type Enzyme Acting on β-1,2-Glucooligosaccharides from Parabacteroides distasonis. Biochemistry. 2018;57(26):3849-3860. DOI:10.1021/acs.biochem.8b00385 |
18. Tanaka N, Nakajima M, Narukawa-Nara M, Matsunaga H, Kamisuki S, Aramasa H, Takahashi Y, Sugimoto N, Abe K, Terada T, Miyanaga A, Yamashita T, Sugawara F, Kamakura T, Komba S, Nakai H, and Taguchi H. (2019). Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family. J Biol Chem. 2019;294(19):7942-7965. DOI:10.1074/jbc.RA118.007087 |