Abstract
Glycodiversification of natural products is an effective strategy for small molecule drug development. Recently, improved methods for chemo-enzymatic synthesis of glycosyl donors has spurred the characterization of natural product glycosyltransferases (GTs), revealing that the substrate specificity of many naturally occurring GTs as too stringent for use in glycodiversification. Protein engineering of natural product GTs has emerged as an attractive approach to overcome this limitation. This review highlights recent progress in the engineering/evolution of enzymes relevant to natural product glycodiversification with a particular focus upon GTs.
Original language | English |
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Pages (from-to) | 556-564 |
Number of pages | 9 |
Journal | Current Opinion in Chemical Biology |
Volume | 12 |
Issue number | 5 |
DOIs | |
State | Published - Oct 2008 |
Bibliographical note
Funding Information:This contribution was supported in part by National Institutes of Health Grants CA84374 and U19 CA113297 (JTS). JST is an H.I. Romnes fellow.
Funding
This contribution was supported in part by National Institutes of Health Grants CA84374 and U19 CA113297 (JTS). JST is an H.I. Romnes fellow.
Funders | Funder number |
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National Institutes of Health (NIH) | U19 CA113297 |
National Institutes of Health (NIH) | |
National Childhood Cancer Registry – National Cancer Institute | R01CA084374 |
National Childhood Cancer Registry – National Cancer Institute |
ASJC Scopus subject areas
- Analytical Chemistry
- Biochemistry