Projects per year
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.
Original language | English |
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Pages (from-to) | 567-597 |
Number of pages | 31 |
Journal | Annual Review of Plant Biology |
Volume | 57 |
DOIs | |
Publication status | Published - 2006 |
Keywords
- detoxification
- homeostasis
- hormones
- secondary metabolites
- stress responses
- CARBOXYPEPTIDASE-LIKE PROTEIN
- ZEATIN O-GLUCOSYLTRANSFERASE
- LEGUME MEDICAGO-TRUNCATULA
- CELL-SUSPENSION CULTURES
- SECALE-CEREALE L
- ARABIDOPSIS-THALIANA
- UDP-GLUCOSE
- SALICYLIC-ACID
- ANTHOCYANIN BIOSYNTHESIS
- HETEROLOGOUS EXPRESSION
Projects
- 2 Finished
-
Glucosyltransferases of the common phenylpropanoid pathway
1/10/04 → 30/09/07
Project: Research project (funded) › Research
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Functional analysis of the glucosylation of auxin abscisic acid and their metabolites in Arabidopsis thaliana
BBSRC (BIOTECHNOLOGY AND BIOLOGICAL SCIENCES RESEARCH COUNCIL)
1/04/04 → 29/02/08
Project: Research project (funded) › Research