Lipoxygenase enzyme a new target for nicotine and rotenone insecticides

Document Type : Original Article

Authors

1 Pesticide Dept., Faculty of Agriculture and Biochemistry Dept.

2 Faculty of Science. University of Alexandria, Alexandria, Egypt.

10.21608/jpces.1990.460588

Abstract

Lipoxygenase (linoleate oxygen oxidoreductase) activity has been measured in the presence and absence of nicotine and rotenone, botanical insecticides. Nicotine inhibits lipoxygenase enzyme with a time and concentration-dependent response with 1st value equal to 5 x 10-7 M concentration. Lineweaver-Burk plot design shows that nicotine inhibits lipoxygenase enzyme with a value of Km equal 0.66 uM in a non-competitive inhibition manner with a Vmax equal 18.5 uM/mg protein/min in the presence of 25 uM of nicotine concentration. Rotenone inhibits lipoxygenase enzyme in a dose-dependent way after a preincubation period between the enzyme protein and rotenone with I50 value equal to 2 x 10-7 M concentration. Rotenone inhibits lipoxygenase enzyme with non-competitive inhibition manner with Km value of 0.66 uM and Vmax 30 and 20 uM/mg protein/ min in absence and presence of 2.5 x 10-5 M concentration. Specific and selective inhibition of lipoxygenase enzyme by nicotine and rotenone is useful not only as a tool for investigating regulatory mechanism of leukotriene biosynthesis but also as a new site of toxicological action of this group of insecticides.