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.

1. Institute for Cellular and Molecular Biology, 1 University Station A4810, University of Texas at Austin, Austin, Texas 78712, USA.
2. Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas at Austin, Austin, Texas 78712, USA.
3. Division of Medicinal Chemistry, College of Pharmacy, 1 University Station A1935, University of Texas at Austin, Austin, Texas 78712, USA.

Correspondence to: H.-w.L. (Email: h.w.liu@mail.utexas.edu).
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