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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Flavanone-specific 7-O-glucosyltransferase activity in Citrus paradisi seedlings: purification and characterization.

The isolation and characterization of a flavanone-specific 7-O-glucosyltransferase and its resolution from other glucosyltransferases in Citrus paradisi (grapefruit) seedlings is described. This new enzyme in the subclass 2.4.1 catalyzes the glucosylation of the 7-OH group of naringenin (4',5',7-trihydroxyflavanone) to prunin and has been purified (943-fold) by fractional precipitation with ammonium sulfate and successive chromatography on Sephadex G-100, hydroxyapatite, UDP-glucuronic acid agarose, Mono Q, and Mono P columns. It has a pH optimum of 7.5-8.0, an apparent pI of 4.3, and an apparent Mr of 54,900. This glucosyltransferase has an expressed specificity for the 7-position of the flavanones naringenin (Kmapp 62 microM; Kmapp UDPG 51 microM) and hesperetin (Kmapp 124 microM; Kmapp UDPG 243 microM) and did not accept other flavone or flavonol aglycones. Characteristics of other flavonoid glucosyltransferase activities found in grapefruit seedlings are also described.[1]

References

  1. Flavanone-specific 7-O-glucosyltransferase activity in Citrus paradisi seedlings: purification and characterization. McIntosh, C.A., Latchinian, L., Mansell, R.L. Arch. Biochem. Biophys. (1990) [Pubmed]
 
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