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- W2127810013 abstract "A “soluble” enzyme system from soybean, which catalyzes the biosynthesis of N-glucosylarylamines, has been purified 20-fold by differential centrifugation, ammonium sulfate fractionation, gel filtration, and cellulose ion exchange chromatography. The enzyme was specific for the nucleotide glucosyl donors uridinediphosphate glucose (UDPG) and thymidinediphosphate glucose (TDPG), but exhibited a broad specificity toward acceptor arylamines. A number of substituted anilines and aminobenzoic acids were studied as acceptor arylamines including 2,5-dichloro-3-aminobenzoic acid (amiben) and 3,4-dichloroaniline, a metabolite of 3,4-dichloropropionanilide (propanil) in higher plants. The partially purified enzyme was found to have an optimum pH of 7·5 with 3,4-dichloroaniline as the arylamine acceptor and was inhibited by sulfhydryl reagents. The Km constants for UDPG and 3,4-dichloroaniline were 1·88 × 10−3 M and 5·63 × 10−4 M respectively. The Ki constant for uridinediphosphate (UDP) was 4·84 × 10−4 M." @default.
- W2127810013 created "2016-06-24" @default.
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- W2127810013 date "1968-03-01" @default.
- W2127810013 modified "2023-10-06" @default.
- W2127810013 title "Herbicide metabolism in plants—I" @default.
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- W2127810013 doi "https://doi.org/10.1016/s0031-9422(00)90876-8" @default.
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