Open AccessAn extracellular enzyme from Fusarium solani f. sp. phaseoli which catalyses hydration of the isoflavonoid phytoalexin, phaseollidin
Author(s) -
Turbek Carol S.,
Smith David A.,
Schardl Christopher L.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05312.x
Subject(s) - isoflavonoid , phytoalexin , fusarium solani , phaseolus , enzyme , chemistry , biochemistry , gel electrophoresis , biology , flavonoid , antioxidant , microbiology and biotechnology , botany , resveratrol
Among the antimicrobial phytoalexins produced by Phaseolus vulgaris (French bean) are the prenylated isoflavonoids kievitone and phaseollidin. Two enzyme activities, kievitone hydratase and phaseollidin hydratase, occur in culture filtrates of the bean pathogen, Fusarium solani f. sp. phaseoli , and catalyse similar hydration reactions on the dimethylallyl moieties of the phytoalexins. The enzymes nearly co‐purified during hydroxyapatite chromatography followed by preparative native gel electrophoresis. Eluates from successive slices taken from the native gel were assayed for both activities. Although they were not completely separated in the native gel, the activity profiles indicated that the two activities were distinct. The K m of phaseollidin hydratase for phaseollidin was approximately 7 μM.