Flavan-3-ol Biosynthesis

Stafford, Helen A.; Lester, Hope H.

doi:10.1104/pp.76.1.184

Cited by 86 publications

(25 citation statements)

References 2 publications

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“…The identity of the minor product as (+)-catechin was unequivocally established by co-migration of the radioactivity with an authentic standard in various chromatographic systems (section 2. NADPH-dependent reactions, have also been reported by STAFFORD and co-workers (12,13,14,15) in connection with proanthocyanidin biosynthesis in cell cultures of Douglas fir needies, and by HELLER et al (7) in connection with anthocyanidin biosynthesis in Matthiola incana. Whereas pH-optima of 7.4 and 6.0 were found for the enzymes involved in proanthocyanidin and anthocyanidin biosynthesis, respectively, the (+)-dihydroquercetin reductase activity from barley grains showed pH-optima at both 7.0 and 6.0.…”

Section: Enzymatic Reduction Of (+)-Dihydro-mentioning

confidence: 63%

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Conversion of (+)-dihydroquercetin to (+)-2,3-trans-3,4-cis-leucocyanidin and (+)-catechin with an enzyme extract from maturing grains of barley

Kristiansen

1986

Carlsberg Res. Commun.

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A soluble, NADPH-dependent reduetase, catalyzing the reduction of(+)-dihydroquercetin to (+) -2,3-trans-3,4-cis-leucocyanidin ((2R,3S,4S)-3,4,5,7,3',4'-hexahydroxyflavan), was demonstrated in an enzyme preparation from maturing grains of wild type barley (Hordeum vulgare L., cv. Nordal). This reductase activity had a oH-optimum around 7.0 and was strongly inhibited by the product of the reaction. Furthermore, a second, less active NADPH-dependent reductase, catalyzing the reduction of(+)-2,3-trans-3,4-cis-leucocyanidin to (+)-catechin, was demonstrated by a double step reduction of (+)-dihydroquercetin to (+)-catechin.The reaction product of(+)-dihydroquercetin reductase was identified by co-chromatography with an authentic standard of (+)-2,3-trans-3,4-cis-leucocyanidin, which was prepared chemically by acid epimerization of (+) -2,3-trans-3,4-trans-leucocyanidin ((2R,3S,4R)-3,4,5,7,Y,4'-hexahydroxyflavan) and characterized by 'H NMR spectroscopy in the free phenolic form.

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Section: Enzymatic Reduction Of (+)-Dihydro-mentioning

confidence: 63%

“…the leucocyanidin to (+)-catechin have been reported by STAFFORD and co-workers (12,13,15) in extracts of cell cultures of Douglas fir needles.…”

Section: (+)-23-trans-34-cis-leucocyanidin and Thenmentioning

confidence: 99%

Conversion of (+)-dihydroquercetin to (+)-2,3-trans-3,4-cis-leucocyanidin and (+)-catechin with an enzyme extract from maturing grains of barley

Kristiansen

1986

Carlsberg Res. Commun.

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“…Several remarkable advances are reported in reviews (12,19,20,36,37). Stafford (20,38,39) revealed that dihydroflavonol 4-reductase and leucoanthocyanidin reductase catalyzed dihydroflavonols to leucoanthocyanidins, then to 2,3-trans-2R,3S-flavan-3-ol (C or GC) and speculated that 2,3-trans-2R,3S-flavan-3-ol was converted to 2,3-cis-2R,3R-flavan-3-ol (EC or EGC) by an epimerase. However, Xie et al (21) reported a new flavan-3-ol biosynthesis pathway in which the anthocyanidin reductase, encoded by the BANYLUS gene in Arabidopsis and Medicago truncatula (21), converted anthocyanidins into their corresponding 2, 3-cis-2R, 3R-flavan-3-ols such as EC, epiafzelechin, and EGC in the presence of NADPH.…”

Section: Galloylation Of Catechins In Teamentioning

confidence: 99%

Purification and Characterization of a Novel Galloyltransferase Involved in Catechin Galloylation in the Tea Plant (Camellia sinensis)

Gao

Liu

et al. 2012

Journal of Biological Chemistry

146

144

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Background: Galloylated catechins, including (Ϫ)-epigallocatechin gallate and (Ϫ)-epicatechin gallate, comprise up to 76% of catechins in tea plant; their biosynthesis is unknown. Results: An enzyme involved in galloylated catechin biosynthesis was purified and identified in tea plant. Conclusion: Galloylated catechin was biosynthesized via a newly discovered enzyme, epicatechin:1-O-galloyl-␤-D-glucose O-galloyltransferase. Significance: This work improves our understanding of flavan-3-ols biosynthesis.

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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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Flavan-3-ol Biosynthesis

Cited by 86 publications

References 2 publications

Conversion of (+)-dihydroquercetin to (+)-2,3-trans-3,4-cis-leucocyanidin and (+)-catechin with an enzyme extract from maturing grains of barley

Conversion of (+)-dihydroquercetin to (+)-2,3-trans-3,4-cis-leucocyanidin and (+)-catechin with an enzyme extract from maturing grains of barley

Purification and Characterization of a Novel Galloyltransferase Involved in Catechin Galloylation in the Tea Plant (Camellia sinensis)

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

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