Oxidative Transformation of Dihydroflavonols and Flavan-3-ols by Anthocyanidin Synthase from Vitis vinifera

Twelve polyphenols from three distinct families (dihydroflavonols, flavan-3-ols, and flavanones) were studied as potential substrates of anthocyanidin synthase from ( ANS). Only flavan-3-ols of (2 ,3 ) configuration having either a catechol or gallol group on ring B are accepted as substrates. Only...

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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2022-02, Vol.27 (3), p.1047
Main Authors: Zhang, Jia-Rong, Trossat-Magnin, Claudine, Bathany, Katell, Negroni, Luc, Delrot, Serge, Chaudière, Jean
Format: Article
Language:English
Subjects:
2-oxoglutarate
anthocyanidin synthase
ascorbate
Ascorbic acid
Biosynthesis
Catechin
Catechol
Configurations
dihydroflavonol
Enzymes
flavanol
Flavonoids
Flavonols
Flavonols - metabolism
High-performance liquid chromatography
Hydroxylation
Life Sciences
Liquid chromatography
Oxidation-Reduction
Oxygenases - metabolism
Physiology
Plant Proteins - metabolism
Polyphenols
Polyphenols - metabolism
Retention
Rings (mathematics)
Substrate Specificity
Substrates
Transformations
Vegetal Biology
Vitis - metabolism
Vitis vinifera
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Summary:Twelve polyphenols from three distinct families (dihydroflavonols, flavan-3-ols, and flavanones) were studied as potential substrates of anthocyanidin synthase from ( ANS). Only flavan-3-ols of (2 ,3 ) configuration having either a catechol or gallol group on ring B are accepted as substrates. Only dihydroflavonols of (2 ,3 ) configuration are accepted as substrates, but a catechol or gallol group is not mandatory. Flavanones are not substrates of ANS. HPLC and MS/MS analyses of the enzymatic products showed that the ANS-catalyzed oxidative transformation of (+)-dihydroflavonols, such as dihydroquercetin, dihydrokaempferol and dihydromyricetin, leads only to the corresponding flavonols. Among the flavan-3-ols recognized as substrates, (+)-gallocatechin was only transformed into delphinidin by ANS, whereas (+)-catechin was transformed into three products, including two major products that were an ascorbate-cyanidin adduct and a dimer of oxidized catechin, and a minor product that was cyanidin. Data from real-time MS monitoring of the enzymatic transformation of (+)-catechin suggest that its products are all derived from the initial C -hydroxylation intermediate, i.e., a 3,3-gem-diol, and their most likely formation mechanism is discussed.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules27031047