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Difference between revisions of "User:Shinya Fushinobu"
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| − | [[Image: | + | [[Image:Fushinobu3.jpg|200px|right]] |
I am a Professor at [http://enzyme13.bt.a.u-tokyo.ac.jp/index-e.html Laboratory of Enzymology] in Department of Biotechnology, [http://www.a.u-tokyo.ac.jp/english/index.html Graduate School of Agricultural and Life Sciences], [http://www.u-tokyo.ac.jp/index_e.html The University of Tokyo] located in Tokyo, Japan. Raised in [http://www.city.kure.hiroshima.jp/site/userguide/foreign.html 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 [http://enzyme13.bt.a.u-tokyo.ac.jp/fushi/index-e.html here]. I contributed to three-dimensional structure determination of | I am a Professor at [http://enzyme13.bt.a.u-tokyo.ac.jp/index-e.html Laboratory of Enzymology] in Department of Biotechnology, [http://www.a.u-tokyo.ac.jp/english/index.html Graduate School of Agricultural and Life Sciences], [http://www.u-tokyo.ac.jp/index_e.html The University of Tokyo] located in Tokyo, Japan. Raised in [http://www.city.kure.hiroshima.jp/site/userguide/foreign.html 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 [http://enzyme13.bt.a.u-tokyo.ac.jp/fushi/index-e.html here]. I contributed to three-dimensional structure determination of | ||
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*[[GH65]] ''Caldicellulosiruptor saccharolyticus'' kojibiose phosphorylase (CsKP) <cite>Okada2013</cite> | *[[GH65]] ''Caldicellulosiruptor saccharolyticus'' kojibiose phosphorylase (CsKP) <cite>Okada2013</cite> | ||
*[[GH65]] ''Bacillus selenitireducens'' 2-''O''-α-glucosylglycerol phosphorylase (GGP) <cite>Touhara2014</cite> | *[[GH65]] ''Bacillus selenitireducens'' 2-''O''-α-glucosylglycerol phosphorylase (GGP) <cite>Touhara2014</cite> | ||
| − | |||
*[[GH94]] ''Vibrio proteolyticus'' chitobiose phosphorylase (ChBP) '''Family First''' <cite>Hidaka2004</cite> | *[[GH94]] ''Vibrio proteolyticus'' chitobiose phosphorylase (ChBP) '''Family First''' <cite>Hidaka2004</cite> | ||
*[[GH94]] ''Cellvibrio gilvus'' cellobiose phosphorylase (CBP) <cite>Hidaka2006</cite> | *[[GH94]] ''Cellvibrio gilvus'' cellobiose phosphorylase (CBP) <cite>Hidaka2006</cite> | ||
*[[GH94]] ''Saccharophagus degradans'' cellobionic acid phosphorylase (CABP) <cite>Nam2015</cite> | *[[GH94]] ''Saccharophagus degradans'' cellobionic acid phosphorylase (CABP) <cite>Nam2015</cite> | ||
| + | *[[GH94]] ''Lachnoclostridium phytofermentans'' 1,2-β-oligoglucan phosphorylase (LpSOGP) <cite>Nakajima2017</cite> | ||
*[[GH101]] ''Bifidobacterium longum'' endo-α-''N''-acetylgalactosaminidase (EngBF) <cite>Suzuki2009</cite> | *[[GH101]] ''Bifidobacterium longum'' endo-α-''N''-acetylgalactosaminidase (EngBF) <cite>Suzuki2009</cite> | ||
*[[GH112]] ''Bifidobacterium longum'' galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) '''Family First''' <cite>Hidaka2009</cite> | *[[GH112]] ''Bifidobacterium longum'' galacto-''N''-biose/lacto-''N''-biose I phosphorylase (GLNBP) '''Family First''' <cite>Hidaka2009</cite> | ||
*[[GH127]] ''Bifidobacterium longum'' β-L-arabinofuranosidase (HypBA1) '''Family First''' <cite>Ito2014</cite> | *[[GH127]] ''Bifidobacterium longum'' β-L-arabinofuranosidase (HypBA1) '''Family First''' <cite>Ito2014</cite> | ||
| + | *[[GH129]] ''Bifidobacterium bifidum'' α-''N''-acetylgalactosaminidase (NagBb) '''Family First''' <cite>Sato2017</cite> | ||
*[[GH130]] ''Listeria innocua'' β-1,2-mannobiose phosphorylase (Lin0857) <cite>Tsuda2015</cite> | *[[GH130]] ''Listeria innocua'' β-1,2-mannobiose phosphorylase (Lin0857) <cite>Tsuda2015</cite> | ||
| − | + | *[[GH136]] ''Bifidobacterium longum'' lacto-''N''-biosidase (LnbX) '''Family First''' <cite>Yamada2017</cite> | |
| + | *[[GH144]] ''Chitinophaga pinensis'' endo-β-1,2-glucanase (Cpin_6279) '''Family First''' <cite>Abe2017</cite> | ||
*[[PL20]] ''Trichoderma reesei'' endo-β-1,4-glucuronan lyase (TrGL) '''Family First''' <cite>Konno2009</cite> | *[[PL20]] ''Trichoderma reesei'' endo-β-1,4-glucuronan lyase (TrGL) '''Family First''' <cite>Konno2009</cite> | ||
*[[CBM28]] in ''Clostridium josui'' Cel5A (''Cj''CBM28) <cite>Tsukimoto2010</cite> | *[[CBM28]] in ''Clostridium josui'' Cel5A (''Cj''CBM28) <cite>Tsukimoto2010</cite> | ||
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#Honda2016 pmid=26621872 | #Honda2016 pmid=26621872 | ||
#Matsuzawa2016 pmid=27092463 | #Matsuzawa2016 pmid=27092463 | ||
| + | #Nakajima2017 pmid=28198470 | ||
| + | #Abe2017 pmid=28270506 | ||
| + | #Yamada2017 pmid=28392148 | ||
| + | #Sato2017 pmid=28546425 | ||
</biblio> | </biblio> | ||
[[Category:Contributors|Fushinobu, Shinya]] | [[Category:Contributors|Fushinobu, Shinya]] | ||
Revision as of 19:52, 22 June 2017
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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- 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 |
- Error fetching PMID 23537284:
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- Error fetching PMID 17383976:
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- Error fetching PMID 24570006:
- 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 |
- Error fetching PMID 12215416:
- Error fetching PMID 26601228:
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- 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 |
- 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 |
- 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 |
- Error fetching PMID 24255995:
- 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 |
- 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 |
- Error fetching PMID 16646954:
- 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 |
- 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 |
- Error fetching PMID 19502354:
- 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 |
- 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 |
- Error fetching PMID 28546425:
- 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 |
- 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 |
- 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 |
- 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 |
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