1gp5: Difference between revisions
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==Overview== | ==Overview== | ||
Flavonoids are common colorants in plants and have long-established, biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate, iron-dependent oxygenase, catalyzes the penultimate step in the, biosynthesis of the anthocyanin class of flavonoids. The crystal structure, of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional, structure obtained after 30 min exposure to dioxygen is consistent with, the oxidation of the dihydroquercetin to quercetin and the concomitant, decarboxylation of 2-oxoglutarate to succinate. Together with in vitro, studies, the crystal structures suggest a mechanism for ANS-catalyzed, anthocyanidin formation from the natural leucoanthocyanidin substrates, .. | Flavonoids are common colorants in plants and have long-established, biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate, iron-dependent oxygenase, catalyzes the penultimate step in the, biosynthesis of the anthocyanin class of flavonoids. The crystal structure, of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional, structure obtained after 30 min exposure to dioxygen is consistent with, the oxidation of the dihydroquercetin to quercetin and the concomitant, decarboxylation of 2-oxoglutarate to succinate. Together with in vitro, studies, the crystal structures suggest a mechanism for ANS-catalyzed, anthocyanidin formation from the natural leucoanthocyanidin substrates, involving stereoselective C-3 hydroxylation. The structure of ANS provides, a template for the ubiquitous family of plant nonhaem oxygenases for, future engineering and inhibition studies. | ||
==About this Structure== | ==About this Structure== | ||
1GP5 is a | 1GP5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with FE, AKG, MES, DQH and DH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: IRN. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GP5 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: flavonoid biosynthesis]] | [[Category: flavonoid biosynthesis]] | ||
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Revision as of 15:08, 5 November 2007
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ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA COMPLEXED WITH TRANS-DIHYDROQUERCETIN
OverviewOverview
Flavonoids are common colorants in plants and have long-established, biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate, iron-dependent oxygenase, catalyzes the penultimate step in the, biosynthesis of the anthocyanin class of flavonoids. The crystal structure, of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional, structure obtained after 30 min exposure to dioxygen is consistent with, the oxidation of the dihydroquercetin to quercetin and the concomitant, decarboxylation of 2-oxoglutarate to succinate. Together with in vitro, studies, the crystal structures suggest a mechanism for ANS-catalyzed, anthocyanidin formation from the natural leucoanthocyanidin substrates, involving stereoselective C-3 hydroxylation. The structure of ANS provides, a template for the ubiquitous family of plant nonhaem oxygenases for, future engineering and inhibition studies.
About this StructureAbout this Structure
1GP5 is a Single protein structure of sequence from Arabidopsis thaliana with FE, AKG, MES, DQH and DH2 as ligands. Structure known Active Site: IRN. Full crystallographic information is available from OCA.
ReferenceReference
Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana., Wilmouth RC, Turnbull JJ, Welford RW, Clifton IJ, Prescott AG, Schofield CJ, Structure. 2002 Jan;10(1):93-103. PMID:11796114
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