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• W2161032012 abstract "The bioactive isoflavonoids of the Leguminosae often are methylated on the 4'-position of their B-rings. Paradoxically, reverse genetic evidence implicates alfalfa isoflavone O-methyltransferase (IOMT) in the biosynthesis of 4'-O-methylated isoflavonoids such as the phytoalexin medicarpin in vivo, whereas biochemical studies indicate that IOMT has strict specificity for methylation of the A-ring 7-hydroxyl of daidzein, the presumed substrate for O-methylation, in vitro. Radiolabeling and isotope dilution studies now confirm that daidzein is not an intermediate in isoflavonoid phytoalexin biosynthesis in alfalfa. Furthermore, protein gel blot analysis and confocal microscopy of a transiently expressed IOMT-green fluorescent protein fusion in alfalfa leaves show that the operationally soluble IOMT localizes to endomembranes after elicitation of the isoflavonoid pathway. We propose that IOMT colocalizes with the endoplasmic reticulum-associated isoflavone synthase cytochrome P450 to ensure rapid B-ring methylation of the unstable 2,4',7-trihydroxyisoflavanone product of isoflavone synthase, thereby preventing its dehydration to daidzein and subsequent A-ring methylation by free IOMT. In this way, metabolic channeling at the entry point into isoflavonoid phytoalexin biosynthesis protects an unstable intermediate from an unproductive metabolic conversion." @default.
• W2161032012 created "2016-06-24" @default.
• W2161032012 creator A5047292984 @default.
• W2161032012 creator A5063052790 @default.
• W2161032012 date "2001-12-01" @default.
• W2161032012 modified "2023-10-17" @default.
• W2161032012 title "Elicitor-Induced Association of Isoflavone <i>O</i>-Methyltransferase with Endomembranes Prevents the Formation and 7-<i>O</i>-Methylation of Daidzein during Isoflavonoid Phytoalexin Biosynthesis" @default.
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• W2161032012 doi "https://doi.org/10.1105/tpc.010382" @default.
• W2161032012 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/139479" @default.
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