Engelhardt G, Wallnöfer P
Zentralbl Bakteriol Orig B. 1976 Jul;162(1-2):138-44.
The phenylurea herbicide linuron is hydrolyzed by Bacillus sphaericus ATCC 12123 quantitatively forming 3,4-dichloroaniline, CO2, and N,O-dimethylhydroxylamine. The inducible enzyme responsible for this hydrolysis was purified to homogeneity as judged by polyacrylamide gel electrophoresis. Its molecular weight was 75 000 +/- 10%. Studies on its substrate specificity showed that either whole cells as the linuron-induced enzyme hydrolyze a large number of herbicidal and fungicidal acylanilides, the methoxysubstituted phenylureas and the phenylcarbamate propham at the carbonyl-aniline bond. This would classify the enzyme as an aryl acylamidase (E.C. 3.5.1). Hydrolysis of phenylamides by whole cells and by the enzyme is inhibited by different methylcarbamate and organophosphorus insecticides. Inhibition of hydrolysis of linuron by the aryl acylamidase by methylcarbamates is a competitive one.
球形芽孢杆菌ATCC 12123可将苯基脲类除草剂利谷隆定量水解，生成3,4 - 二氯苯胺、二氧化碳和N,O - 二甲基羟胺。经聚丙烯酰胺凝胶电泳判断，负责这种水解反应的诱导酶已被纯化至同质。其分子量为75000±10%。对其底物特异性的研究表明，无论是作为利谷隆诱导酶的全细胞，还是该酶本身，均可在羰基 - 苯胺键处水解大量除草和杀真菌酰基苯胺、甲氧基取代的苯基脲以及苯基氨基甲酸酯类除草剂苯胺灵。这表明该酶可归类为芳基酰基酰胺酶（酶学委员会编号3.5.1）。全细胞和该酶对苯基酰胺的水解受到不同氨基甲酸甲酯和有机磷杀虫剂的抑制。氨基甲酸甲酯对芳基酰基酰胺酶催化利谷隆水解的抑制作用属于竞争性抑制。
