The enzyme catalyses the formation of the additional ring in pterocarpan, the basic structure of phytoalexins produced by leguminous plants, including (–)-medicarpin, (+)-medicarpin, (–)-maackiain and (+)-maackiain. The enzyme requires that the hydroxyl group at C-4 of the substrate is in the (4R) configuration. The configuration of the hydrogen atom at C-3 determines whether the pterocarpan is the (+)- or (–)-enantiomer. The enzyme contains amino acid motifs characteristic of dirigent proteins.
The enzyme appears in viruses and cellular organisms
The enzyme catalyses the formation of the additional ring in pterocarpan, the basic structure of phytoalexins produced by leguminous plants, including (-)-medicarpin, (+)-medicarpin, (-)-maackiain and (+)-maackiain. The enzyme requires that the hydroxyl group at C-4 of the substrate is in the (4R) configuration. The configuration of the hydrogen atom at C-3 determines whether the pterocarpan is the (+)- or (-)-enantiomer. The enzyme contains amino acid motifs characteristic of dirigent proteins.
the ethylene-insensitive strain A17 mutant sickle (skl) with a point mutation in the EIN2 gene is highly susceptible to Rhizoctonia solani strain AG8 and shows no transcriptional response of the isoflavonoid-related genes. The skl mutant of strain A17 shows no induction of the amounts of medicarpin or 7,4'-dihydroxyflavone, by ethylene, but accumulates isoprenoid precursors of the defense molecules, e.g. the precursor of medicarpin. Overexpression of the isoflavonoid pathway increases the resistance against root pathogen Rhizoctonia solani strain AG8. No compensation of the phenotype by medicarpin addition
the ethylene-insensitive strain A17 mutant sickle (skl) with a point mutation in the EIN2 gene is highly susceptible to Rhizoctonia solani strain AG8 and shows no transcriptional response of the isoflavonoid-related genes. The skl mutant of strain A17 shows no induction of the amounts of medicarpin or 7,4'-dihydroxyflavone, by ethylene, but accumulates isoprenoid precursors of the defense molecules, e.g. the precursor of medicarpin. Overexpression of the isoflavonoid pathway increases the resistance against root pathogen Rhizoctonia solani strain AG8. No compensation of the phenotype by medicarpin addition
strain A17 shows accumulation of phytoalexin medicarpin, as well as of other isoflavonoid-related compounds like liquiritigenin, formononetin, and biochanin A. The strain is resistant against Rhizoctonia solani infection. Medicarpin is derived from the isoflavonoid-based biosynthesis pathway and involved in plant defense. Rhizoctonia solani strain AG8 infection induces the defense genes by production of ethylene. The enzyme is involved in ethylene-iduced plant defense against root pathogens
strain A17 shows accumulation of phytoalexin medicarpin, as well as of other isoflavonoid-related compounds like liquiritigenin, formononetin, and biochanin A. The strain is resistant against Rhizoctonia solani infection. Medicarpin is derived from the isoflavonoid-based biosynthesis pathway and involved in plant defense. Rhizoctonia solani strain AG8 infection induces the defense genes by production of ethylene. The enzyme is involved in ethylene-iduced plant defense against root pathogens
the skl mutant of strain A17 shows no induction of the enzyme, or amounts of medicarpin or 7,4'-dihydroxyflavone, by ethylene, but accumulates isoprenoid precursors of the defense molecules, e.g. the precursor of medicarpin. Overexpression of the isoflavonoid pathway increases the resistance against root pathogen Rhizoctonia solani strain AG8. No compensation of the phenotype by medicarpin addition
the skl mutant of strain A17 shows no induction of the enzyme, or amounts of medicarpin or 7,4'-dihydroxyflavone, by ethylene, but accumulates isoprenoid precursors of the defense molecules, e.g. the precursor of medicarpin. Overexpression of the isoflavonoid pathway increases the resistance against root pathogen Rhizoctonia solani strain AG8. No compensation of the phenotype by medicarpin addition
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the activities of vestitone reductase and 7,2'-dihydroxy-4'-methoxyisoflavanol dehydratase increase approximately 3fold 6 hours after elicitor treatment in alfalfa suspension cell culture. The activities remain at maximal levels for 40 hours, correlating with a steady increase in the medicarpin content of the cells
The pterocarpan synthase of alfalfa: association and co-induction of vestitone reductase and 7,2-dihydroxy-4-methoxy-isoflavanol (DMI) dehydratase, the two final enzymes in medicarpin biosynthesis
Conversion of vestitone to medicarpin in alfalfa (Medicago sativa L.) is catalyzed by two independent enzymes. Identification, purification, and characterization of vestitone reductase and 7,2-dihydroxy-4-methoxyisoflavanol dehydratase
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