The biochemical basis for l-canavanine tolerance by the tobacco budworm Heliothis virescens (Noctuidae)

Abstract

The tobacco budworm, Heliothis virescens (Noctuidae), a destructive insect pest, is remarkably resistant to l-canavanine, l-2-amino-4-(guanidinooxy)butyric acid, an arginine antimetabolite that is a potent insecticide for nonadapted species. H. virescens employs a constitutive enzyme of the larval gut, known trivially as canavanine hydrolase (CH), to catalyze an irreversible hydrolysis of l-canavanine to l-homoserine and hydroxyguanidine. As such, it represents a new type of hydrolase, one acting on oxygen–nitrogen bonds (EC 3.13.1.1). This enzyme has been isolated from the excised gut of H. virescens and purified to homogeneity; it exhibits an apparent K _m value for l-canavanine of 1.1 mM and a turnover number of 21.1 μmol·min⁻¹·μmol⁻¹. This enzyme has a mass of 285 kDa and is composed of two subunits with a mass of 50 kDa or 47.5 kDa. CH has a high degree of specificity for l-canavanine as it cannot function effectively with either l-2-amino-5-(guanidinooxy)pentanoate or l-2-amino-3-(guanidinooxy)propionate, the higher or lower homolog of l-canavanine, respectively. l-Canavanine derivatives such as methyl-l-canavanine, or l-canaline and O-ureido-l-homoserine, are not metabolized significantly by CH.

• allelochemical detoxification