Abstract
A glutathione S-transferase (GST) which catalyses the conjugation of cinnamic acid with glutathione has been partially characterized from suspension cultured cells of French bean ( Phaseolus vulgaris) and other legume species. The glutathione S-cinnamoyl transferases (GSCTs) appeared to be distinct from other plant GSTs and showed a species-dependent subcellular distribution between the cytosol and microsomes. The enzyme from legumes was inhibited by known inhibitors of plant GSTs, and cross-reacted with an antiserum raised against a cytosolic GST from Zea mays which is involved in herbicide detoxification. Bean GSCT was a cytosolic enzyme with a K m of 330 μM for cinnamic acid. Its activity was unaffected by treating cells with cinnamic acid but was increased two- to three-fold by exposure of the cells to an elicitor preparation from the cell walls of the fungal bean pathogen Colletotrichum lindemuthianum.
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