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Difference between revisions of "User:Sei Motouchi"
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(biochemical identification and determination of Michaelis complex) | (biochemical identification and determination of Michaelis complex) | ||
| + | [[GH186]] ''Xanthomonas campestris'' pv. ''campestris'' α-1,6-cyclized β-1,2-glucohexadecaose synthase (XccOpgD) '''First-identified anomer-inverting transglycosylase''' <cite>Motouchi2024</cite>. | ||
| + | (biochemical identification, determination of Michaelis complex and Suggestion of reaction mechanism) | ||
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<biblio> | <biblio> | ||
#Motouchi2023 pmid=37735577 | #Motouchi2023 pmid=37735577 | ||
| + | #Motouchi2024 pmid=38957137 | ||
</biblio> | </biblio> | ||
Revision as of 20:17, 7 July 2024
I am a Ph. D candidate at Tokyo university of science. My research interests concern structure and function of new CAZymes, especially β-1,2-glucan-related enzymes responsible for enabling interactions between organisms. I contributed to the biochemical identification and/or structural determination of
GH186 Escherichia coli endo β-1,2-glucanase (EcOpgD) Family first [1].
(biochemical identification, determination of Michaelis complex and Suggestion of unique reaction mechanism)
GH186 Escherichia coli endo β-1,2-glucanase (EcOpgG) [1].
(biochemical identification and determination of Michaelis complex)
GH186 Xanthomonas campestris pv. campestris α-1,6-cyclized β-1,2-glucohexadecaose synthase (XccOpgD) First-identified anomer-inverting transglycosylase [2].
(biochemical identification, determination of Michaelis complex and Suggestion of reaction mechanism)
- 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 |
- Motouchi S, Komba S, Nakai H, and Nakajima M. (2024). Discovery of Anomer-Inverting Transglycosylase: Cyclic Glucohexadecaose-Producing Enzyme from Xanthomonas, a Phytopathogen. J Am Chem Soc. 2024;146(26):17738-17746. DOI:10.1021/jacs.4c02579 |