Abstract
Saturation transfer difference (STD) NMR experiments reveal the binding epitopes of UDP-Gal and UDP-Glc bound to the glycosyltransferase β4Gal-T1 (see picture). Whereas the enzyme recognizes the galactose residue in UDP-Gal, it does not make any close contacts with the glucose residue in UDP-Glc. This observation explains why β4Gal-T1 binds to UDP-Glc but is unable to transfer glucose to an acceptor substrate.
| Original language | English |
|---|---|
| Journal | Angewandte Chemie - International Edition |
| Volume | 40 |
| Issue number | 22 |
| Pages (from-to) | 4189-4192 |
| Number of pages | 4 |
| ISSN | 1433-7851 |
| DOIs | |
| Publication status | Published - 19.11.2001 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
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