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Unusual sugar biosynthesis and natural product glycodiversification

Author

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  • Christopher J. Thibodeaux

    (Institute for Cellular and Molecular Biology, 1 University Station A4810, University of Texas at Austin)

  • Charles E. Melançon

    (1 University Station A5300, University of Texas at Austin)

  • Hung-wen Liu

    (Institute for Cellular and Molecular Biology, 1 University Station A4810, University of Texas at Austin
    1 University Station A5300, University of Texas at Austin
    College of Pharmacy, 1 University Station A1935, University of Texas at Austin)

Abstract

The enzymes involved in the biosynthesis of carbohydrates and the attachment of sugar units to biological acceptor molecules catalyse an array of chemical transformations and coupling reactions. In prokaryotes, both common sugar precursors and their enzymatically modified derivatives often become substituents of biologically active natural products through the action of glycosyltransferases. Recently, researchers have begun to harness the power of these biological catalysts to alter the sugar structures and glycosylation patterns of natural products both in vivo and in vitro. Biochemical and structural studies of sugar biosynthetic enzymes and glycosyltransferases, coupled with advances in bioengineering methodology, have ushered in a new era of drug development.

Suggested Citation

  • Christopher J. Thibodeaux & Charles E. Melançon & Hung-wen Liu, 2007. "Unusual sugar biosynthesis and natural product glycodiversification," Nature, Nature, vol. 446(7139), pages 1008-1016, April.
  • Handle: RePEc:nat:nature:v:446:y:2007:i:7139:d:10.1038_nature05814
    DOI: 10.1038/nature05814
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    Cited by:

    1. Min Li & Yang Zhou & Zexing Wen & Qian Ni & Ziqin Zhou & Yiling Liu & Qiang Zhou & Zongchao Jia & Bin Guo & Yuanhong Ma & Bo Chen & Zhi-Min Zhang & Jian-bo Wang, 2024. "An efficient C-glycoside production platform enabled by rationally tuning the chemoselectivity of glycosyltransferases," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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