info:eu-repo/semantics/article
Identification of a Bifunctional Maize C- and O-Glucosyltransferase
Fecha
2013-10Registro en:
Falcone Ferreyra, María Lorena; Rodriguez, Eduardo Jose; Casas, María Isabel; Labadie, Guillermo Roberto; Grotewold, Erich; et al.; Identification of a Bifunctional Maize C- and O-Glucosyltransferase; American Society For Biochemistry And Molecular Biology; Journal Of Biological Chemistry; 288; 44; 10-2013; 31678-31688
0021-9258
Autor
Falcone Ferreyra, María Lorena
Rodriguez, Eduardo Jose
Casas, María Isabel
Labadie, Guillermo Roberto
Grotewold, Erich
Casati, Paula
Resumen
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.