Bombyx mori-derived aldo-keto reductase AKR2E8 detoxifies aldehydes present in mulberry leaves.

Lepidopterans are agricultural pests. Since the silkworm is a model for lepidopterans, analysis of the enzymes produced by silkworms is of great interest for developing methods of pest control. The aldo-keto reductase (AKR) superfamily catalyzes the reduction of aldehydes by converting a carbonyl group to an alcohol group. Here, we characterized a new AKR present in the silkworm Bombyx mori, which has been designated as AKR2E8. Amino acid sequence and phylogenetic analyses showed that AKR2E8 is similar to human AKR1B1 and AKR1B10. Three amino acid residues in the active site were identical among AKR2E8, AKR1B1, and AKR1B10. Recombinant AKR2E8 overexpressed in Escherichia coli used nicotinamide adenine dinucleotide phosphate as a coenzyme to reduce the aldehydes present in mulberry (Morus alba) leaves. AKR2E8 was found to reduce benzaldehyde, hexanal, heptanal, nonanal, trans-2-nonenal, and citral. No nicotinamide adenine dinucleotide-dependent activity was detected. Akr2e8 mRNA was detected in the testes, ovaries, and fat body; the highest expression was found in the midgut. The substrate specificity and highest observed expression of AKR2E8 in the midgut suggests that AKR2E8 may play a major role in aldehyde detoxification in silkworms. The findings of this study may assist in the development of pest control methods for controlling the population of lepidopterans, such as silkworms, that damage crops.