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Glycosyltransferases: managers of small molecules
Dianna Bowles1, Judith Isayenkova, Eng-Kiat Lim
1Centre for Novel Agricultural Products (CNAP), Department of Biology, University of York, York YO10 5DD, UK. wjs3@york.ac.uk
Current Opinion in Plant Biology
|April 30, 2005
Summary
Glycosyltransferases (GTs) are enzymes that modify small molecules. Recent advances have improved our understanding of GTs
Area of Science:
- Biochemistry and Molecular Biology
- Plant Science
- Enzymology
Background:
- Glycosyltransferases (GTs) are crucial enzymes involved in attaching sugar moieties to various acceptor molecules.
- Recent advancements in gene identification and activity characterization have significantly boosted research into small molecule GTs.
- These enzymes play vital roles in plants, influencing metabolism, detoxification, and signaling pathways.
Purpose of the Study:
- To review the recent progress in understanding the function and application of glycosyltransferases (GTs).
- To highlight the diverse roles of GTs in modifying plant metabolites, xenobiotics, and phytotoxins.
- To explore the potential of GTs as biocatalysts due to their specific recognition and catalytic properties.
Main Methods:
- Literature review of recent studies on glycosyltransferases.
- Analysis of gene identification techniques for GTs.
- Characterization of GTs' catalytic activities and substrate specificities.
Main Results:
- Glycosylation by GTs significantly alters the physicochemical properties (e.g., hydrophilicity, stability) of acceptor molecules.
- GTs exhibit broad substrate recognition, including plant metabolites, phytotoxins, and xenobiotics.
- Glycosylation impacts the subcellular localization and bioactivity of modified compounds.
Conclusions:
- Significant progress has been made in understanding the roles of GTs in plant systems.
- GTs are valuable biocatalysts due to their regio- and enantioselectivity.
- The ability of GTs to act on non-plant metabolites expands their utility beyond natural plant processes.
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