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Difference between revisions of "User:Tomomi Sumida"
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Tomomi Sumida obtained her Ph.D. from [http://www.agr.kyushu-u.ac.jp/english/ the Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyusyu University], under the supervision of Professor Makoto Ito in 2010. She isolated the ganglioside–degrading bacterium ''Paenibacillus'' sp. strain TS12 from land soil in her doctoral research <cite>SumidaAEM2002</cite>. Strain TS12 produces a series of glycosphingolipid-degrading enzymes, such as sialidase, β-galactosidase, β-hexosaminidase, β-''N''-acetylgalactosaminidase, and β-glucocerebrosidase. She has reported the molecular cloning, characterization, and structural analysis of these novel glycosphingolipid-degrading enzymes, as follows: | Tomomi Sumida obtained her Ph.D. from [http://www.agr.kyushu-u.ac.jp/english/ the Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyusyu University], under the supervision of Professor Makoto Ito in 2010. She isolated the ganglioside–degrading bacterium ''Paenibacillus'' sp. strain TS12 from land soil in her doctoral research <cite>SumidaAEM2002</cite>. Strain TS12 produces a series of glycosphingolipid-degrading enzymes, such as sialidase, β-galactosidase, β-hexosaminidase, β-''N''-acetylgalactosaminidase, and β-glucocerebrosidase. She has reported the molecular cloning, characterization, and structural analysis of these novel glycosphingolipid-degrading enzymes, as follows: | ||
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* [[GH123]] β-''N''-acetylgalactosaminidase (NgaP) from ''Paenibacillus'' sp. TS12 <cite>SumidaJBC2011</cite>. | * [[GH123]] β-''N''-acetylgalactosaminidase (NgaP) from ''Paenibacillus'' sp. TS12 <cite>SumidaJBC2011</cite>. | ||
| − | NgaP, which specifically hydrolyzes the non-reducing terminal β-GalNAc linkage but not β-GlcNAc linkage, is the first β-''N''-acetylgalactosaminidase (EC 3.2.1.53) to have its primary structure elucidated. Since the primary structure of NgaP is totally new, | + | NgaP, which specifically hydrolyzes the non-reducing terminal β-GalNAc linkage but not β-GlcNAc linkage, is the first β-''N''-acetylgalactosaminidase (EC 3.2.1.53) to have its primary structure elucidated. Since the primary structure of NgaP is totally new, [http://www.cazy.org/GH123.html GH123] was created as a new family of β-''N''-acetylgalactosaminidases in 2011. |
Latest revision as of 02:39, 11 August 2016
Tomomi Sumida obtained her Ph.D. from the Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyusyu University, under the supervision of Professor Makoto Ito in 2010. She isolated the ganglioside–degrading bacterium Paenibacillus sp. strain TS12 from land soil in her doctoral research [1]. Strain TS12 produces a series of glycosphingolipid-degrading enzymes, such as sialidase, β-galactosidase, β-hexosaminidase, β-N-acetylgalactosaminidase, and β-glucocerebrosidase. She has reported the molecular cloning, characterization, and structural analysis of these novel glycosphingolipid-degrading enzymes, as follows:
- GH3 β-glucocerebrosidase (Glc4) from Paenibacillus sp. TS12 [2].
- GH20 β-hexosaminidase (Hex1) from Paenibacillus sp. TS12 [3, 4].
- GH123 β-N-acetylgalactosaminidase (NgaP) from Paenibacillus sp. TS12 [5].
NgaP, which specifically hydrolyzes the non-reducing terminal β-GalNAc linkage but not β-GlcNAc linkage, is the first β-N-acetylgalactosaminidase (EC 3.2.1.53) to have its primary structure elucidated. Since the primary structure of NgaP is totally new, GH123 was created as a new family of β-N-acetylgalactosaminidases in 2011.
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- Sumida T, Fujimoto K, and Ito M. (2011). Molecular cloning and catalytic mechanism of a novel glycosphingolipid-degrading beta-N-acetylgalactosaminidase from Paenibacillus sp. TS12. J Biol Chem. 2011;286(16):14065-72. DOI:10.1074/jbc.M110.182592 |