Detoxifying enzymes of the brown planthopper (BPH).
1993
Chien Jung Gu | Wen Lin Chen | Chin Ning Sun
Considerable conjugation of 1-chloro-2,4-dinitrobenzene mediated by glutathione transferase has been observed in BPH. This enzyme in the pest, however, does not show any detectable activity toward another model substrate, 1,2-dichloro-4-nitrobenzene, or insecticides (parathion, paraoxon, and methyl parathion) known to be substrates for glutathione trasferase in other insects. Activity of microsomal P450-dependent monooxygenase toward several model substrates in BPH is very low - only about 1/50 to 1/100 of that in some lepidopterous insects. It has been hypothesized that this low monooxygenase activity may be due to its contact with only water-soluble materials in plant sap. The metabolic mechanisms of insecticide resistance observed in BPH may reflect the fundamental makeup of detoxifying enzymes. A lack of cross-resistance in BPH from existing organophosphorus/pyrethroid resistance to buprofezin might be because the carboxylesterases do not hydrolize this chitin synthesis inhibitor. Further, there may not be active microsomal monooxygenases with which to hydroxylate buprofezin, a known detoxifying reaction observed in soils.
Show more [+] Less [-]AGROVOC Keywords
Bibliographic information
This bibliographic record has been provided by Wolters Kluwer