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Difference between revisions of "User:Masahiro Nakajima"

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'''This is an empty template to help you get started with composing your User page.'''
 
  
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 is an assistant professor in Taguchi Laboratory at Department of Applied Biological Science, Tokyo University of Science (2012-). 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 144 and 162. He determined the functions and/or crystal structures of  
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[https://www.rs.tus.ac.jp/m-nakajima/index.html 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. [[User:Motomitsu Kitaoka|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]]''' and '''[[GH189]]''' and also created '''clan GH-S'''. He determined the functions and/or crystal structures of  
  
* GH3 β-Glucosidases [1-3]
+
* [[GH3]] β-Glucosidases <cite>Nakajima2012a Nakajima2016 Ishiguro2017</cite>
* GH16 β-1,3-Glucanase [4]
+
* [[GH16]] β-1,3-Glucanase <cite>Nakajima2012b</cite>
* GH38 α-mannosidase [5]
+
* [[GH35]] β-1,2-Glucosyltransglycosylase <cite>Kobayashi2022</cite> ('''[https://www.enzyme-database.org/query.php?ec=2.4.1.391 new EC number]''')
* GH57 4-α-glucanotransferase [6]
+
* [[GH38]] α-Mannosidase <cite>Nakajima2003</cite>
* GH94 1,2-β-Oligoglucan phosphorylase [7,8]
+
* [[GH57]] 4-α-Glucanotransferase <cite>Nakajima2004</cite>
* GH112 D-Galactosyl-β-1,4-L-rhamnose phosphorylase and β-1,3-galactosyl-N-acetylhexosamine phosphorylase [9-12]
+
* [[GH94]] 1,2-β-Oligoglucan phosphorylases <cite>Nakajima2017 Nakajima2014</cite> ('''[https://www.enzyme-database.org/query.php?ec=2.4.1.333 new EC number]''')
 
+
* [[GH112]] D-Galactosyl-β-1,4-L-rhamnose phosphorylase <cite>Nakajima2009a</cite> ('''[https://www.enzyme-database.org/query.php?ec=2.4.1.247 new EC number]''') and β-1,3-galactosyl-''N''-acetylhexosamine phosphorylases <cite>Nakajima2009a Nakajima2009b Nakajima2008a Nakajima2008b</cite>
* GH144 Bacterial β-1,2-Glucanases [13,14]
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* [[GH144]] Bacterial β-1,2-glucanases <cite>Abe2017</cite> ('''family created''') and sophorosylhydrolase <cite>Shimizu2018</cite> ('''[https://www.enzyme-database.org/query.php?ec=3.2.1.214 new EC number]''')
* GH162 Fungal β-1,2-Glucanase [15]
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* [[GH162]] Fungal β-1,2-glucanase <cite>Tanaka2019</cite> ('''family created''') ('''clan GH-S created''')
 +
* [[GH186]] ''E. coli'' β-1,2-glucanase <cite>Motouchi2023</cite> ('''family created''')
 +
* [[GH189]] Cyclic β-1,2-glucan synthase (transglycosylase domain) <cite>Tanaka2024</cite> ('''family created''')
  
  
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<biblio>
 
<biblio>
#Nakajima2012  pmid=21850431
+
#Nakajima2012a  pmid=21850431
 
#Nakajima2016  pmid=26886583
 
#Nakajima2016  pmid=26886583
 
#Ishiguro2017  pmid=29131329
 
#Ishiguro2017  pmid=29131329
#Nakajima2012  pmid=22685137
+
 
 +
#Nakajima2012b  pmid=22685137
 
#Nakajima2003  pmid=12801516
 
#Nakajima2003  pmid=12801516
 
#Nakajima2004  pmid=15564678
 
#Nakajima2004  pmid=15564678
#Nakajima2012  pmid=22685137
+
 
 
#Nakajima2017  pmid=28198470
 
#Nakajima2017  pmid=28198470
#Nakajima2016   pmid=24647662
+
#Nakajima2014   pmid=24647662
 +
 
 
#Nakajima2009a  pmid=19491100
 
#Nakajima2009a  pmid=19491100
 
#Nakajima2009b  pmid=19132369
 
#Nakajima2009b  pmid=19132369
 
#Nakajima2008a  pmid=18723650
 
#Nakajima2008a  pmid=18723650
 
#Nakajima2008b  pmid=18183385
 
#Nakajima2008b  pmid=18183385
 +
 
#Abe2017        pmid=28270506
 
#Abe2017        pmid=28270506
 
#Shimizu2018    pmid=29763309
 
#Shimizu2018    pmid=29763309
 
#Tanaka2019    pmid=30926603
 
#Tanaka2019    pmid=30926603
 +
#Kobayashi2022  pmid=35065074
 +
#Motouchi2023  pmid=37735577
 +
#Tanaka2024    pmid=38300345
 +
 +
  
 
</biblio>
 
</biblio>

Latest revision as of 06:29, 19 March 2024

Candidate2png.png

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 and GH189 and also created clan GH-S. He determined the functions and/or crystal structures of

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



  1. 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 | PubMed ID:21850431 [Nakajima2012a]
  2. 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 | PubMed ID:26886583 [Nakajima2016]
  3. 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 | PubMed ID:29131329 [Ishiguro2017]
  4. 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 | PubMed ID:22685137 [Nakajima2012b]
  5. Kobayashi K, Shimizu H, Tanaka N, Kuramochi K, Nakai H, Nakajima M, and Taguchi H. (2022). Characterization and structural analyses of a novel glycosyltransferase acting on the β-1,2-glucosidic linkages. J Biol Chem. 2022;298(3):101606. DOI:10.1016/j.jbc.2022.101606 | PubMed ID:35065074 [Kobayashi2022]
  6. 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 | PubMed ID:12801516 [Nakajima2003]
  7. 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 | PubMed ID:15564678 [Nakajima2004]
  8. 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 | PubMed ID:28198470 [Nakajima2017]
  9. 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 | PubMed ID:24647662 [Nakajima2014]
  10. 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 | PubMed ID:19491100 [Nakajima2009a]
  11. 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 | PubMed ID:19132369 [Nakajima2009b]
  12. 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 | PubMed ID:18723650 [Nakajima2008a]
  13. 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 | PubMed ID:18183385 [Nakajima2008b]
  14. 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 | PubMed ID:28270506 [Abe2017]
  15. 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 | PubMed ID:29763309 [Shimizu2018]
  16. 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 | PubMed ID:30926603 [Tanaka2019]
  17. Motouchi S, Kobayashi K, Nakai H, and Nakajima M. (2023). Identification of enzymatic functions of osmo-regulated periplasmic glucan biosynthesis proteins from Escherichia coli reveals a novel glycoside hydrolase family. Commun Biol. 2023;6(1):961. DOI:10.1038/s42003-023-05336-6 | PubMed ID:37735577 [Motouchi2023]
  18. Tanaka N, Saito R, Kobayashi K, Nakai H, Kamo S, Kuramochi K, Taguchi H, Nakajima M, and Masaike T. (2024). Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase. Appl Microbiol Biotechnol. 2024;108(1):187. DOI:10.1007/s00253-024-13013-9 | PubMed ID:38300345 [Tanaka2024]

All Medline abstracts: PubMed