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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 147 (1987), S. 201-206 
    ISSN: 1432-072X
    Keywords: Degradation ; Pterocarpan ; Phytoalexins ; Medicarpin ; Ascochyta rabiei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Four strains of Ascochyta rabiei pathogenic to chickpea (Cicer arietinum L.) were shown to efficiently degrade medicarpin (3-hydroxy-9-methoxypterocarpan), the main phytoalexin of this plant. Degradative studies were performed with mycelium preparations or with crude protein extracts of the fungus. Isolation and structural elucidation of 10 catabolites by chromatographic and spectroscopic techniques revealed that medicarpin degradation involves 1. reductive conversion to a 2′-hydroxyisoflavan, 2. O-demethylation, 3. aromatic hydroxylation in ring A and 4. formation of a 1a-hydroxy-pterocarp-1,4-diene-3-one. As terminal aromatic catabolite 2,4-dihydroxybenzoic acid was found. A catabolic sequence for medicarpin is postulated and the results are discussed with regard to pterocarpan dissimilation by other phytopathogenic fungi.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Metabolism ; Pterocarpan ; Phytoalexins ; Ascochyta rabiei ; Monooxygenase ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Crude protein extracts from the chickpea (Cicer arietinum) pathogenic fungus Ascochyta rabiei catalyze the hydroxylation of the pterocarpan phytoalexins medicarpin and maackiain to the corresponding 1a-hydroxy-1,4-diene-3-one derivatives. The enzyme reaction depends on NAD(P)H and molecular oxygen. Low amounts of FAD are necessary for maximal enzyme activity. The pterocarpan hydroxylase is a new flavoprotein monooxygenase with a molecular weight of 58 kDa in SDS-PAGE. The soluble enzyme can utilize NADH and NADPH with similar values for K m and V max respectively. The pterocarpan hydroxylase and a pterocarpan reductase (M r 29 kDa; Höhl and Barz 1987) are constitutively expressed by A. rabiei isolates.
    Type of Medium: Electronic Resource
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