Recent advances in the biosynthesis and accumulation of anthocyanins

Springob, Karin; Nakajima, Jun–ichiro; Yamazaki, Mami; Saito, Kazuki

doi:10.1039/b109542k

Cited by 334 publications

(231 citation statements)

References 149 publications

(146 reference statements)

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“…As such it catalyses the last common step in the biosynthesis of the most abundant flavonoids, i.e. flavan-3-ols and condensed tannins [9][10][11][12][13][14][15][16][17][18]. Because of this strategic position, DFRs with distinct substrate specificities may exert an important control on the pattern of anthocyanins and proanthocyanidins which are produced downstream.…”

Section: Introductionmentioning

confidence: 99%

Kinetic and binding equilibrium studies of dihydroflavonol 4-reductase from Vitis vinifera and its unusually strong substrate inhibition

Trabelsi¹,

d’Estaintot²,

Sigaud³

et al. 2011

JBPC

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Dihydroflavonol 4-reductase (DFR), a member of the short-chain dehydrogenase family, catalyzes the last common step in the biosynthesis of flavan-3-ols and condensed tannins. Initial rates of DFR were measured by monitoring the 340-nm absorbance decrease resulting from the joint consumption of dihydroquercetin (DHQ) and NADPH, as a function of pH, temperature and ionic strength. At pH 6.5 and 30˚C, substrate inhibition was observed above 30 µM DHQ. At lower/non-inhibitory DHQ concentrations, NADP + behaves as a competitive inhibitor with respect to NADPH and as a mixed inhibitor with respect to DHQ, which supports a sequential ordered mechanism, with NADPH binding first and NADP + released last. Binding-equilibrium data obtained by means of the chromatographic method of Hummel and Dreyer at pH 7.5 and by isothermal calorimetric titration at pH 6.5 led to the conclusion that ligands of the apoenzyme included NADPH, NADP + and DHQ. The mechanism which best accounts for substrate inhibition at pH 6.5 in the absence of product involves the formation of a binary non-productive E.DHQ complex. Thus, a productive ternary complex cannot be formed when DHQ binds first. This mechanism of inhibition may prevent the accumulation of unstable leucoanthocyanidins within cells.

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Section: Introductionmentioning

confidence: 99%

Kinetic and binding equilibrium studies of dihydroflavonol 4-reductase from Vitis vinifera and its unusually strong substrate inhibition

Trabelsi¹,

d’Estaintot²,

Sigaud³

et al. 2011

JBPC

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“…Proanthocyanidins are present in the fruits, bark, leaves, and seeds of many plants (Dixon et al 2005). Both anthocyanins and proanthocyanidins are localized in the vacuole; however, the enzymatic steps of their synthesis occur in the cytoplasm Springob et al 2003). Glutathione S-transferase (GST) plays a role in the vacuolar transport of anthocyanins, and it is represented by Bz2 in maize (Marrs et al 1995) and AN9 in petunia (Alfenito et al 1998).…”

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confidence: 99%

Characterization of PAP1-upregulated Glutathione S-transferase genes in Arabidopsis thaliana

Wangwattana

Koyama

Nishiyama

et al. 2008

Plant Biotechnology

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Glutathione S-transferase (GST) plays an important role in the transport and accumulation of anthocyanin and proanthocyanidin in plants. In our previous study on Arabidopsis thaliana overexpressing the PRODUCTION OF ANTHOCYANIN PIGMENT 1 (PAP1) gene encoding an MYB transcription factor, the AtGSTF5 and AtGSTF6 genes encoding GST-like protein were up-regulated along with TRANSPARENT TESTA 19 (TT19), which is required for the accumulation of anthocyanin and proanthocyanidin. The proteins encoded by these 3 genes showed very weak GST activities as detected by using recombinant proteins expressed in Escherichia coli. The anthocyanin levels were severely decreased in the tt19 mutant but not in the Atgstf6 mutant, suggesting that TT19 is almost exclusively involved in anthocyanin accumulation. The results of co-expression network analysis using public transcriptome data corresponded to the proposition of the predominant role of TT19 in anthocyanin accumulation.

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“…The flavonoid biosynthetic pathway has been extensively studied in plants by a combination of genetic and labeling studies (7)(8)(9). Advances in genetic techniques and recombinant expression technologies have enabled proposals regarding the substrate and product selectivities of individual enzymes to be studied in vitro.…”

mentioning

confidence: 99%

Mechanistic Studies on Three 2-Oxoglutarate-dependent Oxygenases of Flavonoid Biosynthesis

Turnbull¹,

Nakajima

Welford³

et al. 2004

Journal of Biological Chemistry

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192

154

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Anthocyanidin synthase (ANS), flavonol synthase (FLS), and flavanone 3␤-hydroxylase (FHT) are involved in the biosynthesis of flavonoids in plants and are all members of the family of 2-oxoglutarate-and ferrous iron-dependent oxygenases. ANS, FLS, and FHT are closely related by sequence and catalyze oxidation of the flavonoid "C ring"; they have been shown to have overlapping substrate and product selectivities. In the initial steps of catalysis, 2-oxoglutarate and dioxygen are thought to react at the ferrous iron center producing succinate, carbon dioxide, and a reactive ferryl intermediate, the latter of which can then affect oxidation of the flavonoid substrate.

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Recent advances in the biosynthesis and accumulation of anthocyanins

Cited by 334 publications

References 149 publications

Kinetic and binding equilibrium studies of dihydroflavonol 4-reductase from Vitis vinifera and its unusually strong substrate inhibition

Kinetic and binding equilibrium studies of dihydroflavonol 4-reductase from Vitis vinifera and its unusually strong substrate inhibition

Characterization of PAP1-upregulated Glutathione S-transferase genes in Arabidopsis thaliana

Mechanistic Studies on Three 2-Oxoglutarate-dependent Oxygenases of Flavonoid Biosynthesis

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