Discovery and structural analysis of glycoside hydrolase family 176 α-1,2 glucosidase from Arthrobacter humicola A8F5
Ryota Yasukochi, Takashi Suzuki, Terumasa Toraya, Keiko Hino, Tetsuya Mori, Toma Kashima, Akimasa Miyanaga, Hikaru Watanabe, Shinya Fushinobu · 2026
Read Discovery and structural analysis of glycoside hydrolase family 176 α-1,2 glucosidase from Arthrobacter humicola A8F5 by Ryota Yasukochi, Takashi Suzuki, Terumasa Toraya, Keiko Hino, Tetsuya Mori, Toma Kashima, Akimasa Miyanaga, Hikaru Watanabe, Shinya Fushinobu (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13671375.txt.
Description
Ryota Yasukochi and co-authors report a new enzyme that cuts a rare sugar bond, in a 2026 study. Sugar-cutting enzymes are picky about the exact link they attack. Enzymes for the common starch links are well known. Those that cut alpha-1,2 links in glucose chains are far less explored.
The enzyme comes from a soil bacterium, Arthrobacter humicola. Tests show it cuts only alpha-1,2 links, and it flips the bond shape as it cuts. The team also solved the three-dimensional shape of the enzyme. It belongs to the glycoside hydrolase family 176, a group with few known members. The work opens a fresh route to tools for rare sugar chemistry.
Catalog record
| CREATOR | Ryota Yasukochi, Takashi Suzuki, Terumasa Toraya, Keiko Hino, Tetsuya Mori, Toma Kashima, Akimasa Miyanaga, Hikaru Watanabe, Shinya Fushinobu |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 55 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |