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Difference between revisions of "User:Nobukiyo Tanaka"
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'''Creation of a new GH162 and GH189 family.''' | '''Creation of a new GH162 and GH189 family.''' | ||
| − | He has identified and characterized ''Talaromyces funiculosus'' ''endo''-β-1,2-glucanase (TfSGL) and determined its 3D structures. TfSGL does not share any homology with known glycoside hydrolases (GH). He demonstrated that the reaction mechanism of TfSGL shows clear differences in the reaction pathways from those of GH enzymes. This leads to the classification of the TfSGL group as a new GH family 162. | + | He has identified and characterized ''Talaromyces funiculosus'' ''endo''-β-1,2-glucanase (TfSGL) and determined its 3D structures. TfSGL does not share any homology with known glycoside hydrolases (GH). He demonstrated that the reaction mechanism of TfSGL shows clear differences in the reaction pathways from those of GH enzymes. This leads to the classification of the TfSGL group as a new GH family 162 <cite>Tanaka2019</cite>. |
| − | Furthermore, in 2024, he performed functional and structural analyses of the cyclization domain of CGS alone from ''Thermoanaerobacter italicus'' (TiCGS<sub>Cy</sub>), identified catalytic residues, and determined its 3D structures. This study showed that TiCGS<sub>Cy</sub> exhibits low sequence homology with known GH enzymes and possesses a unique catalytic reaction mechanism. Consequently, the CGSs group is defined as a new GH family 189. | + | Furthermore, in 2024, he performed functional and structural analyses of the cyclization domain of CGS alone from ''Thermoanaerobacter italicus'' (TiCGS<sub>Cy</sub>), identified catalytic residues, and determined its 3D structures. This study showed that TiCGS<sub>Cy</sub> exhibits low sequence homology with known GH enzymes and possesses a unique catalytic reaction mechanism. Consequently, the CGSs group is defined as a new GH family 189 <cite>Tanaka2024</cite>. |
'''Creation of a new clan GH-S.''' | '''Creation of a new clan GH-S.''' | ||
| − | + | He revealed that the overall structure of TfSGL is similar to a prokaryotic ''endo''-β-1,2-glucanase (CpSGL, belonging to GH144), and one of the catalytic residues overlaps significantly. This finding suggested that TfSGL (GH162) and CpSGL (GH144) constitute a new clan GH-S <cite>Tanaka2019, Abe2017, Tanaka2024</cite>. | |
* [[GH162]] ''Talaromyces funiculosus'' (fungal) ''endo''-β-1,2-glucanase <cite>Tanaka2019</cite> | * [[GH162]] ''Talaromyces funiculosus'' (fungal) ''endo''-β-1,2-glucanase <cite>Tanaka2019</cite> | ||
Revision as of 22:13, 7 February 2024
Nobukiyo Tanaka received a Ph.Dr. in Science from Tokyo University of Science under the supervision of Dr. Hayao Taguchi and Dr. Masahiro Nakajima in 2019. He is currently an assistant professor at the same university.
Creation of a new GH162 and GH189 family.
He has identified and characterized Talaromyces funiculosus endo-β-1,2-glucanase (TfSGL) and determined its 3D structures. TfSGL does not share any homology with known glycoside hydrolases (GH). He demonstrated that the reaction mechanism of TfSGL shows clear differences in the reaction pathways from those of GH enzymes. This leads to the classification of the TfSGL group as a new GH family 162 [1].
Furthermore, in 2024, he performed functional and structural analyses of the cyclization domain of CGS alone from Thermoanaerobacter italicus (TiCGSCy), identified catalytic residues, and determined its 3D structures. This study showed that TiCGSCy exhibits low sequence homology with known GH enzymes and possesses a unique catalytic reaction mechanism. Consequently, the CGSs group is defined as a new GH family 189 [2].
Creation of a new clan GH-S.
He revealed that the overall structure of TfSGL is similar to a prokaryotic endo-β-1,2-glucanase (CpSGL, belonging to GH144), and one of the catalytic residues overlaps significantly. This finding suggested that TfSGL (GH162) and CpSGL (GH144) constitute a new clan GH-S [1, 2, 3].
- GH162 Talaromyces funiculosus (fungal) endo-β-1,2-glucanase [1]
- GH189 [2]
- Clan GH-S GH144 and GH162 [2]
- 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 |
- 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 |
- 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 |