2RH8

Structure of apo anthocyanidin reductase from vitis vinifera

Summary for 2RH8

• Entry DOI: 10.2210/pdb2rh8/pdb
• Descriptor: Anthocyanidin reductase, CHLORIDE ION (3 entities in total)
• Functional Keywords: flavonoids, rossmann fold, short chain dehydrogenase/reductase, oxidoreductase
• Biological source: Vitis vinifera (Grape)
• Total number of polymer chains: 1
• Total formula weight: 36839.74

Authors

Gargouri, M.,Mauge, C.,Langlois D'Estaintot, B.,Granier, T.,Manigan, C.,Gallois, B. (deposition date: 2007-10-08, release date: 2008-11-18, Last modification date: 2023-08-30)

Primary citation

Gargouri, M.,Manigand, C.,Mauge, C.,Granier, T.,Langlois d'Estaintot, B.,Cala, O.,Pianet, I.,Bathany, K.,Chaudiere, J.,Gallois, B.
Structure and epimerase activity of anthocyanidin reductase from Vitis vinifera.
Acta Crystallogr.,Sect.D, 65:989-1000, 2009

PubMed Abstract: Together with leucoanthocyanidin reductase, anthocyanidin reductase (ANR) is one of the two enzymes of the flavonoid-biosynthesis pathway that produces the flavan-3-ol monomers required for the formation of proanthocyanidins or condensed tannins. It has been shown to catalyse the double reduction of anthocyanidins to form 2R,3R-flavan-3-ols, which can be further transformed to the 2S,3R isomers by non-enzymatic epimerization. ANR from grape (Vitis vinifera) was expressed in Escherichia coli and purified. Unexpectedly, RP-HPLC, LC-MS and NMR experiments clearly established that the enzyme produces a 50:50 mixture of 2,3-cis and 2,3-trans flavan-3-ols which have been identified by chiral chromatography to be 2S,3S- and 2S,3R-flavan-3-ols, i.e. the naturally rare (+)-epicatechin and (-)-catechin, when cyanidin is used as the substrate of the reaction. The first three-dimensional structure of ANR is described at a resolution of 2.2 A and explains the inactivity of the enzyme in the presence of high salt concentrations.

PubMed: 19690377
DOI: 10.1107/S0907444909025013

Experimental method

X-RAY DIFFRACTION (2.22 Å)