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Many small molecules are decorated with a variety of substituents as part of their biosynthesis, and until recently, complex glycosylation patterns were considered simply that, complex. New analytical approaches have demonstrated how precise these glycosylation patterns can be, physiological studies have shown how important glycosylation is for both accumulation and the biological activities of small molecules in plants, and recent studies have begun to dissect the biochemical mechanisms responsible for their biosynthesis. However, what has remained baffling is the large number of genes annotated as glucosyltransferases in plant genome sequencing projects.
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In this Paper of the Week, Keiko Yonekura-Sakakibara and colleagues perform a comprehensive assessment of one particular glucosyltransferase. Their data provide both in vitro and in vivo functional characterization of the UGT89C1 locus in Arabidopsis as a flavonol 7-O-rhamnosyltransferase and ties the biochemical specificity of the encoded enzyme to a specific family of glycosylated flavonoids found in planta. The authors have also used informatics tools to define gene networks associated with metabolite accumulation, as well as to model and infer mechanistic features about this newly defined enzyme relative to previous reports of glucosyltransferases.
FOOTNOTES
See referenced article, J. Biol. Chem. 2007, 282, 14932-14941 ![]()
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