Metabolism of substituted diphenylether herbicides in plants. I. Enzymatic cleavage of FLUORODIFEN (cas 15457-05-3) in peas (Pisum sativum L.)

Add time:08/22/2019    Source:sciencedirect.com

A “soluble” glutathione S-transferase that catalyzes the cleavage of the herbicide, 2,4′-dinitro-4-trifluoromethyl diphenylether (FLUORODIFEN (cas 15457-05-3)), was isolated and partially characterized from epicotyl tissues of pea seedlings. A 32-fold purification of the enzyme was achieved by differential centrifugation, ammonium sulfate precipitation, Sephadex gel filtration, and DEAE-cellulose ion exchange chromatography. The enzyme had a pH optimum of 9.3–9.5 and was specific for reduced glutathione, with an estimated apparent Km value of 7.4 × 10−4M. Limited specificity studies with four substituted 14C-labeled diphenylether compounds indicated that fluorodifen was the only effective substrate, with an estimated apparent Km value of 1.2 × 10−5M. Differences and similarities between the pea epicotyl enzyme and other plant and animal glutathione S-transferases were discussed from the standpoint of substrate specificity, pH optima, distribution, stability, and inhibitor studies.

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