Chemoenzymatic synthesis of UDP-GlcNAc and UDP-GalNAc analogs for the preparation of unnatural glycosaminoglycans

Authors
Masuko, S.
Bera, S.
Green, D.E.
Weïwer, M.
DeAngelis, P.L.
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2012
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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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.
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
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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