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Presentation
Expression and Biochemical Characterization of Two Glucosyltransferases from Citrus paradisi
51st Annual Meeting of the Phytochemical Society of North America
  • Shivakumar P. Devaiah, East Tennessee State University
  • Cecelia A. McIntosh, East Tennessee State University
Document Type
Presentation
Publication Date
8-12-2012
Description
Glucosylation is a common alteration reaction in plant metabolism and is regularly associated with the production of secondary metabolites. Glucosylation serves a number of roles within metabolism including: stabilizing structures, affecting solubility, transport, and regulating the bioavailability of the compounds for other metabolic processes. The enzymes that lead to glucoside formation are known as glucosyltransferases (GTs), and characteristically accomplish this task by transferring a UDP-activated glucose to a corresponding acceptor molecule. GTs involved in secondary metabolism share a conserved 44 amino acid residue motif (60–80% identity) known as the plant secondary product glucosyltransferase (PSPG) box, which has been demonstrated to include the UDP-sugar binding moiety. Among the secondary metabolites, flavonoid glycosides and limonoid glycosides affect taste characteristics in citrus making the associated glucosyltransferases particularly interesting targets for biotechnology applications in these species. The research focus of our lab is to establish the function of putative secondary product glucosyltransferase clones identified from Citrus paradisi. In the present study, we report on the activity and biochemical characterization of two clones, PGT 7 (Flavonol-3-O-GT) and PGT8 (Limonoid GT) which were expressed in Pichia pastoris.
Location
London, ON, Canada
Citation Information
Shivakumar P. Devaiah and Cecelia A. McIntosh. "Expression and Biochemical Characterization of Two Glucosyltransferases from Citrus paradisi" 51st Annual Meeting of the Phytochemical Society of North America (2012)
Available at: http://works.bepress.com/cecilia-mcintosh/45/