Abstract
Glycosyltransferases (GTs) are ubiquitous in nature and are required for the transfer of sugars to a variety of important biomolecules. This essential enzyme family has been a focus of attention from both the perspective of a potential drug target and a catalyst for the development of vaccines, biopharmaceuticals and small molecule therapeutics. This review attempts to consolidate the emerging lessons from Leloir (nucleotide-dependent) GT structural biology studies and recent applications of these fundamentals toward rational engineering of glycosylation catalysts.
Original language | English |
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Pages (from-to) | 800-808 |
Number of pages | 9 |
Journal | Current Opinion in Biotechnology |
Volume | 22 |
Issue number | 6 |
DOIs | |
State | Published - Dec 2011 |
Bibliographical note
Funding Information:The unpublished work presented was supported by NIH (AI52218, CA84374 and GM074901) and the Laura and Edward Kremers Chair in Natural Products Chemistry (J.S.T.). We thank Prof. Gavin Williams (NCSU Dept. Chem.) for helpful discussion and review of this manuscript and also Craig Bingman and other members of the Center for Eukaryotic Structural Genomics.
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Biomedical Engineering