Chemoenzymatic synthesis of UDP-GlcNAc and UDP-GalNAc analogs for the preparation of unnatural glycosaminoglycans
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Authors
Masuko, S.
Bera, S.
Green, D.E.
Weïwer, M.
DeAngelis, P.L.
Linhardt, Robert J.
Issue Date
2012
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
Abstract
Eight N-acetylglucosamine-1-phosphate and N-acetylgalactosamine-1-phosphate analogs have been synthesized chemically and were tested for their recognition by the GlmU uridyltransferase enzyme. Among these, only substrates that have an amide linkage to the C-2 nitrogen were transferred by GlmU to afford their corresponding uridine diphosphate(UDP)-sugar nucleotides. Resin-immobilized GlmU showed comparable activity to non-immobilized GlmU and provides a more facile final step in the synthesis of an unnatural UDP-donor. The synthesized unnatural UDP-donors were tested for their activity as substrates for glycosyltransferases in the preparation of unnatural glycosaminoglycans in vitro. A subset of these analogs was useful as donors, increasing the synthetic repertoire for these medically important polysaccharides.
Description
Journal of Organic Chemistry, 77, 1449-1456
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Full Citation
Chemoenzymatic synthesis of UDP-GlcNAc and UDP-GalNAc analogs for the preparation of unnatural glycosaminoglycans, S. Masuko, S. Bera, D. E. Green, M. Weïwer, P. L. DeAngelis, R. J. Linhardt, Journal of Organic Chemistry, 77, 1449-1456, 2012.