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J Biol Chem. 2013 Nov 1;288(44):31678-88. doi: 10.1074/jbc.M113.510040. Epub 2013 Sep 17.

Identification of a bifunctional maize C- and O-glucosyltransferase.

Author information

1
From the Centro de Estudios Fotosintéticos y Bioquímicos.

Abstract

Flavonoids accumulate in plant vacuoles usually as O-glycosylated derivatives, but several species can also synthesize flavonoid C-glycosides. Recently, we demonstrated that a flavanone 2-hydroxylase (ZmF2H1, CYP93G5) converts flavanones to the corresponding 2-hydroxy derivatives, which are expected to serve as substrates for C-glycosylation. Here, we isolated a cDNA encoding a UDP-dependent glycosyltransferase (UGT708A6), and its activity was characterized by in vitro and in vivo bioconversion assays. In vitro assays using 2-hydroxyflavanones as substrates and in vivo activity assays in yeast co-expressing ZmF2H1 and UGT708A6 show the formation of the flavones C-glycosides. UGT708A6 can also O-glycosylate flavanones in bioconversion assays in Escherichia coli as well as by in vitro assays with the purified recombinant protein. Thus, UGT708A6 is a bifunctional glycosyltransferase that can produce both C- and O-glycosidated flavonoids, a property not previously described for any other glycosyltransferase.

KEYWORDS:

Flavonoids; Glycosylation; Glycosyltransferases; Maysin; Metabolic Engineering; Plant Biochemistry

PMID:
24045947
PMCID:
PMC3814763
DOI:
10.1074/jbc.M113.510040
[Indexed for MEDLINE]
Free PMC Article
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