Enzymatic hydroxylation of 6'-deoxychalcones with protein preparations from petals of Dahlia variabilis

Gabrielle Wimmer; Heidrun Halbwirth; Friedrich Wurst; Gert Forkmann; Karl Stich

doi:10.1016/S0031-9422(98)80063-0

Enzymatic hydroxylation of 6'-deoxychalcones with protein preparations from petals of Dahlia variabilis

Gabrielle Wimmer, Heidrun Halbwirth, Friedrich Wurst, Gert Forkmann, Karl Stich

Life Sciences

Technical University of Vienna

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Yellow colouration of Dahlia variabilis flowers is mainly based on isoliquiritigenin and butein 4'-malonylglucosides. Microsomal preparations from petals of the yellow strain 'Johann Nestroy' catalyse the enzymatic 3- hydroxylation of isoliquiritigenin to butein in the presence of NADPH. The reaction showed a pH optimum of 7.5, and was inhibited by p- hydroxymercuribenzoate and a number of cytochrome P450 specific inhibitors. These and further properties suggest that the 3-hydroxylation of isoliquiritigenin is mediated by a cytochrome P450-dependent monooxygenase. The apparent K(m) value for isoliquiritigenin was 50 μM.

Original language	English
Pages (from-to)	1013-1016
Number of pages	4
Journal	Phytochemistry
Volume	47
Issue number	6
DOIs	https://doi.org/10.1016/S0031-9422(98)80063-0
State	Published - Mar 1998

Keywords

6'-deoxychalcone 3- hydroxylase (CH3H)
Biosynthesis
Chalcone
Compositae
Dahlia variabilis

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10.1016/S0031-9422(98)80063-0

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title = "Enzymatic hydroxylation of 6'-deoxychalcones with protein preparations from petals of Dahlia variabilis",

abstract = "Yellow colouration of Dahlia variabilis flowers is mainly based on isoliquiritigenin and butein 4'-malonylglucosides. Microsomal preparations from petals of the yellow strain 'Johann Nestroy' catalyse the enzymatic 3- hydroxylation of isoliquiritigenin to butein in the presence of NADPH. The reaction showed a pH optimum of 7.5, and was inhibited by p- hydroxymercuribenzoate and a number of cytochrome P450 specific inhibitors. These and further properties suggest that the 3-hydroxylation of isoliquiritigenin is mediated by a cytochrome P450-dependent monooxygenase. The apparent K(m) value for isoliquiritigenin was 50 μM.",

keywords = "6'-deoxychalcone 3- hydroxylase (CH3H), Biosynthesis, Chalcone, Compositae, Dahlia variabilis",

author = "Gabrielle Wimmer and Heidrun Halbwirth and Friedrich Wurst and Gert Forkmann and Karl Stich",

year = "1998",

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doi = "10.1016/S0031-9422(98)80063-0",

language = "English",

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pages = "1013--1016",

journal = "Phytochemistry",

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TY - JOUR

T1 - Enzymatic hydroxylation of 6'-deoxychalcones with protein preparations from petals of Dahlia variabilis

AU - Wimmer, Gabrielle

AU - Halbwirth, Heidrun

AU - Wurst, Friedrich

AU - Forkmann, Gert

AU - Stich, Karl

PY - 1998/3

Y1 - 1998/3

N2 - Yellow colouration of Dahlia variabilis flowers is mainly based on isoliquiritigenin and butein 4'-malonylglucosides. Microsomal preparations from petals of the yellow strain 'Johann Nestroy' catalyse the enzymatic 3- hydroxylation of isoliquiritigenin to butein in the presence of NADPH. The reaction showed a pH optimum of 7.5, and was inhibited by p- hydroxymercuribenzoate and a number of cytochrome P450 specific inhibitors. These and further properties suggest that the 3-hydroxylation of isoliquiritigenin is mediated by a cytochrome P450-dependent monooxygenase. The apparent K(m) value for isoliquiritigenin was 50 μM.

AB - Yellow colouration of Dahlia variabilis flowers is mainly based on isoliquiritigenin and butein 4'-malonylglucosides. Microsomal preparations from petals of the yellow strain 'Johann Nestroy' catalyse the enzymatic 3- hydroxylation of isoliquiritigenin to butein in the presence of NADPH. The reaction showed a pH optimum of 7.5, and was inhibited by p- hydroxymercuribenzoate and a number of cytochrome P450 specific inhibitors. These and further properties suggest that the 3-hydroxylation of isoliquiritigenin is mediated by a cytochrome P450-dependent monooxygenase. The apparent K(m) value for isoliquiritigenin was 50 μM.

KW - 6'-deoxychalcone 3- hydroxylase (CH3H)

KW - Biosynthesis

KW - Chalcone

KW - Compositae

KW - Dahlia variabilis

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U2 - 10.1016/S0031-9422(98)80063-0

DO - 10.1016/S0031-9422(98)80063-0

M3 - Article

AN - SCOPUS:0031896512

SN - 0031-9422

VL - 47

SP - 1013

EP - 1016

JO - Phytochemistry

JF - Phytochemistry

IS - 6

ER -

Enzymatic hydroxylation of 6'-deoxychalcones with protein preparations from petals of Dahlia variabilis

Abstract

Keywords

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