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Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification.
EMBO J. 2006 Mar 22; 25(6):1396-405.EJ

Abstract

Glycosylation is a key mechanism for orchestrating the bioactivity, metabolism and location of small molecules in living cells. In plants, a large multigene family of glycosyltransferases is involved in these processes, conjugating hormones, secondary metabolites, biotic and abiotic environmental toxins, to impact directly on cellular homeostasis. The red grape enzyme UDP-glucose:flavonoid 3-O-glycosyltransferase (VvGT1) is responsible for the formation of anthocyanins, the health-promoting compounds which, in planta, function as colourants determining flower and fruit colour and are precursors for the formation of pigmented polymers in red wine. We show that VvGT1 is active, in vitro, on a range of flavonoids. VvGT1 is somewhat promiscuous with respect to donor sugar specificity as dissected through full kinetics on a panel of nine sugar donors. The three-dimensional structure of VvGT1 has also been determined, both in its 'Michaelis' complex with a UDP-glucose-derived donor and the acceptor kaempferol and in complex with UDP and quercetin. These structures, in tandem with kinetic dissection of activity, provide the foundation for understanding the mechanism of these enzymes in small molecule homeostasis.

Authors+Show Affiliations

Department of Chemistry, University of York, York, UK.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16482224

Citation

Offen, Wendy, et al. "Structure of a Flavonoid Glucosyltransferase Reveals the Basis for Plant Natural Product Modification." The EMBO Journal, vol. 25, no. 6, 2006, pp. 1396-405.
Offen W, Martinez-Fleites C, Yang M, et al. Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. EMBO J. 2006;25(6):1396-405.
Offen, W., Martinez-Fleites, C., Yang, M., Kiat-Lim, E., Davis, B. G., Tarling, C. A., Ford, C. M., Bowles, D. J., & Davies, G. J. (2006). Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. The EMBO Journal, 25(6), 1396-405.
Offen W, et al. Structure of a Flavonoid Glucosyltransferase Reveals the Basis for Plant Natural Product Modification. EMBO J. 2006 Mar 22;25(6):1396-405. PubMed PMID: 16482224.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification. AU - Offen,Wendy, AU - Martinez-Fleites,Carlos, AU - Yang,Min, AU - Kiat-Lim,Eng, AU - Davis,Benjamin G, AU - Tarling,Chris A, AU - Ford,Christopher M, AU - Bowles,Dianna J, AU - Davies,Gideon J, Y1 - 2006/02/16/ PY - 2005/08/19/received PY - 2006/01/04/accepted PY - 2006/2/17/pubmed PY - 2006/4/28/medline PY - 2006/2/17/entrez SP - 1396 EP - 405 JF - The EMBO journal JO - EMBO J VL - 25 IS - 6 N2 - Glycosylation is a key mechanism for orchestrating the bioactivity, metabolism and location of small molecules in living cells. In plants, a large multigene family of glycosyltransferases is involved in these processes, conjugating hormones, secondary metabolites, biotic and abiotic environmental toxins, to impact directly on cellular homeostasis. The red grape enzyme UDP-glucose:flavonoid 3-O-glycosyltransferase (VvGT1) is responsible for the formation of anthocyanins, the health-promoting compounds which, in planta, function as colourants determining flower and fruit colour and are precursors for the formation of pigmented polymers in red wine. We show that VvGT1 is active, in vitro, on a range of flavonoids. VvGT1 is somewhat promiscuous with respect to donor sugar specificity as dissected through full kinetics on a panel of nine sugar donors. The three-dimensional structure of VvGT1 has also been determined, both in its 'Michaelis' complex with a UDP-glucose-derived donor and the acceptor kaempferol and in complex with UDP and quercetin. These structures, in tandem with kinetic dissection of activity, provide the foundation for understanding the mechanism of these enzymes in small molecule homeostasis. SN - 0261-4189 UR - https://www.unboundmedicine.com/medline/citation/16482224/Structure_of_a_flavonoid_glucosyltransferase_reveals_the_basis_for_plant_natural_product_modification_ L2 - https://doi.org/10.1038/sj.emboj.7600970 DB - PRIME DP - Unbound Medicine ER -