Literature

Abstract

Fatty acid hydroperoxide lyase (HPL) is a key enzyme in the biosynthesis of plant volatiles involved in defense responses to mechanical or herbivore-induced wounding. We report here the synthesis of imidazole derivatives and their inhibitory activities on the tomato 13-HPL subfamily. Among 11 newly synthesized compounds, we found that 1-[2-benzyloxy-2-(2,4-dichlorophenyl)ethyl]-1H-imidazole (3) exhibits inhibitory activity against recombinant 13-HPL with an IC50 value of approximately 39 mM. Optical difference spectroscopy analysis of compound 3 and HPL interaction indicated that this compound induces a type II binding spectra with a Kd value of approximately 13.5 mM.

DOI： 10.1584/jpestics.G10-66

Biological evaluation of imidazole derivatives as inhibitors of hydroperoxide lyase, a key enzyme in plant volatile biosynthesis

Journal of Pesticide Science 2011.0

Synthesis, biochemical evaluation and rationalisation of the inhibitory activity of a range of 4-substituted phenyl alkyl imidazole-based inhibitors of the enzyme complex 17α-hydroxylase/17,20-lyase (P45017α)

Bioorganic & Medicinal Chemistry Letters 2006.0

Synthesis and biochemical evaluation of a range of potent benzyl imidazole-based compounds as potential inhibitors of the enzyme complex 17α-hydroxylase/17,20-lyase (P45017α)

Bioorganic & Medicinal Chemistry Letters 2006.0

Structure features of imidazole derivatives that enhance styrene oxide hydrolase activity in rat hepatic microsomes

Journal of Medicinal Chemistry 1985.0

Easy and rapid preparation of benzoylhydrazides and their diazene derivatives as inhibitors of 15-lipoxygenase

Bioorganic & Medicinal Chemistry Letters 2017.0

Synthesis and biochemical evaluation of a range of sulfonated derivatives of 4-hydroxybenzyl imidazole as highly potent inhibitors of rat testicular 17α-hydroxylase/17,20-lyase (P-45017α)