GLYCOSYLTRANSFERASES OF LIPOPHILIC SMALL MOLECULES

GLYCOSYLTRANSFERASES OF LIPOPHILIC SMALL MOLECULES Abstract Glycosyltransferases of small molecules transfer sugars to a wide range of acceptors, from hormones and secondary metabolites to biotic and abiotic chemicals and toxins in the environment. The enzymes are encoded by large multigene families and can be identified by a signature motif in their primary sequence, which classifies them as a subset of Family 1 glycosyltransferases. The transfer of a sugar onto a lipophilic acceptor changes its chemical properties, alters its bioactivity, and enables access to membrane transporter systems. In vitro studies have shown that a single gene product can glycosylate multiple substrates of diverse origins; multiple enzymes can also glycosylate the same substrate. These features suggest that in a cellular context, substrate availability is a determining factor in enzyme function, and redundancy depends on the extent of coordinate gene regulation. This review discusses the role of these glycosyltransferases in underpinning developmental and metabolic plasticity during adaptive responses. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Plant Biology Annual Reviews

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Publisher
Annual Reviews
Copyright
Copyright © 2006 by Annual Reviews. All rights reserved
ISSN
1040-2519
DOI
10.1146/annurev.arplant.57.032905.105429
Publisher site
See Article on Publisher Site

Abstract

Abstract Glycosyltransferases of small molecules transfer sugars to a wide range of acceptors, from hormones and secondary metabolites to biotic and abiotic chemicals and toxins in the environment. The enzymes are encoded by large multigene families and can be identified by a signature motif in their primary sequence, which classifies them as a subset of Family 1 glycosyltransferases. The transfer of a sugar onto a lipophilic acceptor changes its chemical properties, alters its bioactivity, and enables access to membrane transporter systems. In vitro studies have shown that a single gene product can glycosylate multiple substrates of diverse origins; multiple enzymes can also glycosylate the same substrate. These features suggest that in a cellular context, substrate availability is a determining factor in enzyme function, and redundancy depends on the extent of coordinate gene regulation. This review discusses the role of these glycosyltransferases in underpinning developmental and metabolic plasticity during adaptive responses.

Journal

Annual Review of Plant BiologyAnnual Reviews

Published: Jun 2, 2006

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