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Difference between revisions of "User:Nobukiyo Tanaka"
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[[Image:Nobukiyo_Tanaka.jpg |200px|right]] | [[Image:Nobukiyo_Tanaka.jpg |200px|right]] | ||
| − | Nobukiyo Tanaka received a Ph. | + | 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. |
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| + | '''Creation of a new GH162 enzyme 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. | ||
| + | |||
| + | '''Creation of a clan GH-S.''' | ||
| + | Furthermore, 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. | ||
| + | |||
| + | '''Creation of a new GH189 enzyme family.''' | ||
| + | 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. | ||
* [[GH162]] ''Talaromyces funiculosus'' (fungal) ''endo''-β-1,2-glucanase <cite>Tanaka2019</cite> | * [[GH162]] ''Talaromyces funiculosus'' (fungal) ''endo''-β-1,2-glucanase <cite>Tanaka2019</cite> | ||
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<biblio> | <biblio> | ||
#Tanaka2019 pmid=30926603 | #Tanaka2019 pmid=30926603 | ||
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</biblio> | </biblio> | ||
<!-- Do not remove this Category tag --> | <!-- Do not remove this Category tag --> | ||
[[Category:Contributors|Tanaka,Nobukiyo]] | [[Category:Contributors|Tanaka,Nobukiyo]] | ||
Revision as of 22:52, 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 enzyme 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.
Creation of a clan GH-S. Furthermore, 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.
Creation of a new GH189 enzyme family. 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.
- 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 |