User:Shinya Fushinobu

I am a Professor at Laboratory of Enzymology in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo located in Tokyo, Japan. Raised in Kure, Hiroshima, Japan. I obtained Ph.D degree in Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo in 1999. My research interests concern structure and function of enzymes, mainly those of Carbohydrate-Active enZymes. My home page is here. I contributed to three-dimensional structure determination of

• GH1 Phanerochaete chrysosporium β-glucosidase 1B (BGL1B) [1]
• GH1 Metagenomic β-Glucosidase (Td2F2) [2]
• GH3 Kluyveromyces marxianus β-glucosidase (KmBglI) [3]
• GH3 Aspergillus aculeatus β-glucosidase (AaBGL1) [4]
• GH8 Bacillus halodurans reducing-end xylose-releasing exo-oligoxylanase (Rex) [5]
• GH9 Photobacterium profundum exo-β-D-glucosaminidase (PpGlcNase) [6]

• GH10 Clostridium stercorarium xylanase B (XynB) [7]
• GH11 Aspergillus kawachii xylanase C (XynC) [8]
• GH20 Bifidobacterium bifidum lacto-N-biosidase (BbLNBase) [9]
• GH26 β-mannanase from a symbiotic protist of the termite Reticulitermes speratus (RsMan26C) [10]
• GH29 Bifidobacterium longum subsp. infantis 1,3-1,4-α-L-fucosidase (BiAfcB) [11]
• GH42 Thermus thermophilus β-galactosidase (A4-β-Gal) Family First [12]
• GH45 Phanerochaete chrysosporium endoglucanase (PcCel45A) [13]

• GH51 Thermotoga maritima α-L-arabinofuranosidase (Tm-AFase) [14]
• GH54 Aspergillus kawachii α-L-arabinofuranosidase B (AkAbfB) Family First plus identification of CBM42 [15]
• GH55 Phanerochaete chrysosporium β-1,3-glucanase (Lam55A) Family First [16]
• GH57 Thermococcus litoralis 4-α-glucanotransferase (TLGT) Family First [17]
• GH65 Caldicellulosiruptor saccharolyticus kojibiose phosphorylase (CsKP) [18]
• GH65 Bacillus selenitireducens 2-O-α-glucosylglycerol phosphorylase (GGP) [19]
• GH94 Vibrio proteolyticus chitobiose phosphorylase (ChBP) Family First [20]
• GH94 Cellvibrio gilvus cellobiose phosphorylase (CBP) [21]
• GH94 Saccharophagus degradans cellobionic acid phosphorylase (CABP) [22]
• GH94 Lachnoclostridium phytofermentans 1,2-β-oligoglucan phosphorylase (LpSOGP) [23]
• GH101 Bifidobacterium longum endo-α-N-acetylgalactosaminidase (EngBF) [24]
• GH112 Bifidobacterium longum galacto-N-biose/lacto-N-biose I phosphorylase (GLNBP) Family First [25]
• GH127 Bifidobacterium longum β-L-arabinofuranosidase (HypBA1) Family First [26]
• GH129 Bifidobacterium bifidum α-N-acetylgalactosaminidase (NagBb) Family First [27]
• GH130 Listeria innocua β-1,2-mannobiose phosphorylase (Lin0857) [28]
• GH136 Bifidobacterium longum lacto-N-biosidase (LnbX) Family First [29]
• GH144 Chitinophaga pinensis endo-β-1,2-glucanase (Cpin_6279) Family First [30]
• PL20 Trichoderma reesei endo-β-1,4-glucuronan lyase (TrGL) Family First [31]
• CBM28 in Clostridium josui Cel5A (CjCBM28) [32]

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1. Nijikken Y, Tsukada T, Igarashi K, Samejima M, Wakagi T, Shoun H, and Fushinobu S. (2007). Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium. FEBS Lett. 2007;581(7):1514-20. DOI:10.1016/j.febslet.2007.03.009 |
2. Matsuzawa T, Jo T, Uchiyama T, Manninen JA, Arakawa T, Miyazaki K, Fushinobu S, and Yaoi K. (2016). Crystal structure and identification of a key amino acid for glucose tolerance, substrate specificity, and transglycosylation activity of metagenomic β-glucosidase Td2F2. FEBS J. 2016;283(12):2340-53. DOI:10.1111/febs.13743 |
3. Yoshida E, Hidaka M, Fushinobu S, Koyanagi T, Minami H, Tamaki H, Kitaoka M, Katayama T, and Kumagai H. (2010). Role of a PA14 domain in determining substrate specificity of a glycoside hydrolase family 3 β-glucosidase from Kluyveromyces marxianus. Biochem J. 2010;431(1):39-49. DOI:10.1042/BJ20100351 |
4. Suzuki K, Sumitani J, Nam YW, Nishimaki T, Tani S, Wakagi T, Kawaguchi T, and Fushinobu S. (2013). Crystal structures of glycoside hydrolase family 3 β-glucosidase 1 from Aspergillus aculeatus. Biochem J. 2013;452(2):211-21. DOI:10.1042/BJ20130054 |
5. 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 |
6. Honda Y, Arai S, Suzuki K, Kitaoka M, and Fushinobu S. (2016). The crystal structure of an inverting glycoside hydrolase family 9 exo-β-D-glucosaminidase and the design of glycosynthase. Biochem J. 2016;473(4):463-72. DOI:10.1042/BJ20150966 |
7. Nishimoto M, Fushinobu S, Miyanaga A, Kitaoka M, and Hayashi K. (2007). Molecular anatomy of the alkaliphilic xylanase from Bacillus halodurans C-125. J Biochem. 2007;141(5):709-17. DOI:10.1093/jb/mvm072 |
8. Fushinobu S, Ito K, Konno M, Wakagi T, and Matsuzawa H. (1998). Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH. Protein Eng. 1998;11(12):1121-8. DOI:10.1093/protein/11.12.1121 |
9. Ito T, Katayama T, Hattie M, Sakurama H, Wada J, Suzuki R, Ashida H, Wakagi T, Yamamoto K, Stubbs KA, and Fushinobu S. (2013). Crystal structures of a glycoside hydrolase family 20 lacto-N-biosidase from Bifidobacterium bifidum. J Biol Chem. 2013;288(17):11795-806. DOI:10.1074/jbc.M112.420109 |
10. Tsukagoshi H, Nakamura A, Ishida T, Touhara KK, Otagiri M, Moriya S, Samejima M, Igarashi K, Fushinobu S, Kitamoto K, and Arioka M. (2014). Structural and biochemical analyses of glycoside hydrolase family 26 β-mannanase from a symbiotic protist of the termite Reticulitermes speratus. J Biol Chem. 2014;289(15):10843-10852. DOI:10.1074/jbc.M114.555383 |
11. Sakurama H, Fushinobu S, Hidaka M, Yoshida E, Honda Y, Ashida H, Kitaoka M, Kumagai H, Yamamoto K, and Katayama T. (2012). 1,3-1,4-α-L-fucosynthase that specifically introduces Lewis a/x antigens into type-1/2 chains. J Biol Chem. 2012;287(20):16709-19. DOI:10.1074/jbc.M111.333781 |
12. 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 |
13. Nakamura A, Ishida T, Kusaka K, Yamada T, Fushinobu S, Tanaka I, Kaneko S, Ohta K, Tanaka H, Inaka K, Higuchi Y, Niimura N, Samejima M, and Igarashi K. (2015). "Newton's cradle" proton relay with amide-imidic acid tautomerization in inverting cellulase visualized by neutron crystallography. Sci Adv. 2015;1(7):e1500263. DOI:10.1126/sciadv.1500263 |
14. Im DH, Kimura K, Hayasaka F, Tanaka T, Noguchi M, Kobayashi A, Shoda S, Miyazaki K, Wakagi T, and Fushinobu S. (2012). Crystal structures of glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermotoga maritima. Biosci Biotechnol Biochem. 2012;76(2):423-8. DOI:10.1271/bbb.110902 |
15. Miyanaga A, Koseki T, Matsuzawa H, Wakagi T, Shoun H, and Fushinobu S. (2004). Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose. J Biol Chem. 2004;279(43):44907-14. DOI:10.1074/jbc.M405390200 |
16. Ishida T, Fushinobu S, Kawai R, Kitaoka M, Igarashi K, and Samejima M. (2009). Crystal structure of glycoside hydrolase family 55 {beta}-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium. J Biol Chem. 2009;284(15):10100-9. DOI:10.1074/jbc.M808122200 |
17. Imamura H, Fushinobu S, Yamamoto M, Kumasaka T, Jeon BS, Wakagi T, and Matsuzawa H. (2003). Crystal structures of 4-alpha-glucanotransferase from Thermococcus litoralis and its complex with an inhibitor. J Biol Chem. 2003;278(21):19378-86. DOI:10.1074/jbc.M213134200 |
18. Okada S, Yamamoto T, Watanabe H, Nishimoto T, Chaen H, Fukuda S, Wakagi T, and Fushinobu S. (2014). Structural and mutational analysis of substrate recognition in kojibiose phosphorylase. FEBS J. 2014;281(3):778-86. DOI:10.1111/febs.12622 |
19. Touhara KK, Nihira T, Kitaoka M, Nakai H, and Fushinobu S. (2014). Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-α-glucosylglycerol phosphorylase. J Biol Chem. 2014;289(26):18067-75. DOI:10.1074/jbc.M114.573212 |
20. 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 |
21. 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 |
22. Nam YW, Nihira T, Arakawa T, Saito Y, Kitaoka M, Nakai H, and Fushinobu S. (2015). Crystal Structure and Substrate Recognition of Cellobionic Acid Phosphorylase, Which Plays a Key Role in Oxidative Cellulose Degradation by Microbes. J Biol Chem. 2015;290(30):18281-92. DOI:10.1074/jbc.M115.664664 |
23. 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 |
24. Suzuki R, Katayama T, Kitaoka M, Kumagai H, Wakagi T, Shoun H, Ashida H, Yamamoto K, and Fushinobu S. (2009). Crystallographic and mutational analyses of substrate recognition of endo-alpha-N-acetylgalactosaminidase from Bifidobacterium longum. J Biochem. 2009;146(3):389-98. DOI:10.1093/jb/mvp086 |
25. 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 |
26. Ito T, Saikawa K, Kim S, Fujita K, Ishiwata A, Kaeothip S, Arakawa T, Wakagi T, Beckham GT, Ito Y, and Fushinobu S. (2014). Crystal structure of glycoside hydrolase family 127 β-l-arabinofuranosidase from Bifidobacterium longum. Biochem Biophys Res Commun. 2014;447(1):32-7. DOI:10.1016/j.bbrc.2014.03.096 |
27. Sato M, Liebschner D, Yamada Y, Matsugaki N, Arakawa T, Wills SS, Hattie M, Stubbs KA, Ito T, Senda T, Ashida H, and Fushinobu S. (2017). The first crystal structure of a family 129 glycoside hydrolase from a probiotic bacterium reveals critical residues and metal cofactors. J Biol Chem. 2017;292(29):12126-12138. DOI:10.1074/jbc.M117.777391 |
28. Tsuda T, Nihira T, Chiku K, Suzuki E, Arakawa T, Nishimoto M, Kitaoka M, Nakai H, and Fushinobu S. (2015). Characterization and crystal structure determination of β-1,2-mannobiose phosphorylase from Listeria innocua. FEBS Lett. 2015;589(24 Pt B):3816-21. DOI:10.1016/j.febslet.2015.11.034 |
29. Yamada C, Gotoh A, Sakanaka M, Hattie M, Stubbs KA, Katayama-Ikegami A, Hirose J, Kurihara S, Arakawa T, Kitaoka M, Okuda S, Katayama T, and Fushinobu S. (2017). Molecular Insight into Evolution of Symbiosis between Breast-Fed Infants and a Member of the Human Gut Microbiome Bifidobacterium longum. Cell Chem Biol. 2017;24(4):515-524.e5. DOI:10.1016/j.chembiol.2017.03.012 |
30. 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 |
31. Konno N, Ishida T, Igarashi K, Fushinobu S, Habu N, Samejima M, and Isogai A. (2009). Crystal structure of polysaccharide lyase family 20 endo-beta-1,4-glucuronan lyase from the filamentous fungus Trichoderma reesei. FEBS Lett. 2009;583(8):1323-6. DOI:10.1016/j.febslet.2009.03.034 |
32. Tsukimoto K, Takada R, Araki Y, Suzuki K, Karita S, Wakagi T, Shoun H, Watanabe T, and Fushinobu S. (2010). Recognition of cellooligosaccharides by a family 28 carbohydrate-binding module. FEBS Lett. 2010;584(6):1205-11. DOI:10.1016/j.febslet.2010.02.027 |