Abstract
Aryl acylamidase (aryl-acylamine amidohydrolase, E.C.3.5.1.13) isolated from lettuce ( Lactuca sativa L.) leaf and stem tissue was assayed using propanil [ N-(3,4-dichlorophenyl)propanamide] as substrate. EPTC ( S-ethyl dipropyl carbamothioate) inhibited aryl acylamidase activity 20 to 65% at concentrations of 10 −4 to 10 −3 M. Kinetic studies indicated a K i of about 4.0 μ M for EPTC. When supplied simultaneously with and at concentrations equal to EPTC, acetone oxime, pyridine-2-aldoxime methiodide, and dimethylglyoxime each reduced the EPTC inhibition of aryl acylamidase activity by about 50%. These oximes alone had little or no effect on aryl acylamidase activity, but another oxime, benzoin-α-oxime, was inhibitory. These results indicate that molecular substituents near the oxime group can alter oxime function related to this class of herbicide safeners.
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