Abstract
The structures of the O-glycosyltransferase LanGT2 and the engineered, C-C bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates.
Original language | English |
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Pages (from-to) | 2811-2815 |
Number of pages | 5 |
Journal | Angewandte Chemie - International Edition |
Volume | 54 |
Issue number | 9 |
DOIs | |
State | Published - Feb 23 2015 |
Bibliographical note
Publisher Copyright:© 2015 Wiley-VCH Verlag GmbH & Co. KGaA.
Keywords
- C-glycosylation
- Carbasugars
- Enzyme engineering
- Friedel-Crafts alkylation
- Glycosyltransferases
ASJC Scopus subject areas
- Catalysis
- General Chemistry