Insights into the stereochemical mechanism of the B12-dependent radical SAM glutamine C- methyltransferase (QCMT)
Thibaut Bourdin, Alain Guillot, Mickaël Mauger, Benjamin Lefranc, Sylvain Gervason, Matthieu Glousieau, Stéphane Grimaldi, Jérôme Leprince, Aurélien Thureau, Alhosna Benjdia, Olivier Berteau · 2026
Read Insights into the stereochemical mechanism of the B12-dependent radical SAM glutamine C- methyltransferase (QCMT) by Thibaut Bourdin, Alain Guillot, Mickaël Mauger, Benjamin Lefranc, Sylvain Gervason, Matthieu Glousieau, Stéphane Grimaldi, Jérôme Leprince, Aurélien Thureau, Alhosna Benjdia, Olivier Berteau (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-13469106.txt.
Description
Thibaut Bourdin and co-authors probe how a vitamin-linked enzyme places methyl marks with a chosen hand in a 2026 study. The enzyme serves a methane-making protein, adding a mark to one of its parts. Its kin can tag plain carbons and pick left from right forms, but what steers the pick was murky.
Tests on several forms of the enzyme split them by how well they grip the vitamin. The steps of grabbing a hydrogen and handing off the methyl run apart, not as one move, so the parts must shift inside the enzyme. The enzyme also made odd marks, flipped forms, and turned one small part into its mirror twin.
Catalog record
| CREATOR | Thibaut Bourdin, Alain Guillot, Mickaël Mauger, Benjamin Lefranc, Sylvain Gervason, Matthieu Glousieau, Stéphane Grimaldi, Jérôme Leprince, Aurélien Thureau, Alhosna Benjdia, Olivier Berteau |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 48 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |