Allelic variants from Dahlia variabilis encode flavonoid 3'-hydroxylases with functional differences in chalcone 3-hydroxylase activity

Archives of Biochemistry and Biophysics
Karin SchlangenHeidi Halbwirth

Abstract

In the petals of Dahlia variabilis, hydroxylation of chalcones at position 3 can be detected, except the well-known flavonoid 3'-hydroxylation. Although the reaction is well characterized at the enzymatic level, it remained unclear whether it is catalyzed by a flavonoid 3'-hydroxylase (F3'H, EC1.14.13.21, CYP75B) with broad substrate specificity. Two novel allelic variants of F3'H were cloned from D. variabilis, which differ only in three amino acids within their 508 residues. The corresponding recombinant enzymes show significant differences in their chalcone 3-hydroxylase (CH3H) activity. A substitution of alanine at position 425 with valine enables CH3H activity, whereas the reciprocal substitution leads to a loss of CH3H activity. Interaction of the valine at position 425 with not yet identified structural properties seems to be decisive for chalcone acceptance. This is the first identification of an F3'H which is able to catalyze chalcone 3-hydroxylation to a physiologically relevant extent from any plant species.

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Citations

Jun 23, 2010·Journal of Experimental Botany·Karin SchlangenHeidi Halbwirth
Apr 14, 2010·International Journal of Molecular Sciences·Heidi Halbwirth
Apr 29, 2015·Planta·Christian SeitzHeidi Halbwirth
Jan 2, 2021·Plant Physiology and Biochemistry : PPB·Benjamin WalliserHeidi Halbwirth
Jul 14, 2017·Phytochemistry·Benjamin BoucherleRomain Haudecoeur

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