Photoaffinity labeling of methyl farnesoate epoxidase in cockroach corpora allata.

摘要: The last enzyme in the biosynthetic pathway to juvenile hormone III corpora allata of hemimetabolous insects is methyl farnesoate epoxidase, a cytochrome P450 monooxygenase. Assays with intact glands incubated vitro and gland homogenates have identified series 1,5-disubstituted imidazoles as potent inhibitors enzyme. We designed, synthesized tested two imidazoles, diazirine-Ice T benzophenone-Ice T, which radiolabeled photoactivatable diazirine or benzophenone group was introduced label hydrophobic substrate binding site Our results show that these bifunctional compounds inhibit JH synthesis by well epoxidation homogenates. Moreover both selectively protein ca. 55 kDa cockroach, Diploptera punctata. These photoaffinity labels, use an imidazole coordinate heme iron photoreactive modify pocket, are specific effective probes for molecular analysis epoxidase.