RRC ID 6109
Author Yamamoto K, Nagaoka S, Banno Y, Aso Y.
Title Biochemical properties of an omega-class glutathione S-transferase of the silkmoth, Bombyx mori.
Journal Comp Biochem Physiol C Toxicol Pharmacol
Abstract A cDNA encoding an omega-class glutathione S-transferase of the silkmoth, Bombyx mori (bmGSTO), was cloned by reverse transcriptase-polymerase chain reaction. The resulting clone was sequenced and deduced for amino acid sequence, which revealed 40, 40, and 39% identities to omega-class GSTs from human, pig, and mouse, respectively. A recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells in a soluble form and purified to homogeneity. rbmGSTO was able to catalyze the biotranslation of glutathione with 1-chloro-2,4-dinitrobenzene, a model substrate for GST, as well as with 4-hydroxynonenal, a product of lipid peroxidation. This enzyme was shown to have high affinity for organophosphorus insecticide and was present abundantly in silkmoth strain exhibiting fenitrothion resistance. These results indicate that bmGSTO could be involved in the increase in level of insecticide resistance for lepidopteran insects.
Volume 149(4)
Pages 461-7
Published 2009-5-1
DOI 10.1016/j.cbpc.2008.10.108
PII S1532-0456(08)00302-5
PMID 19022397
MeSH Amino Acid Sequence Animals Bombyx / enzymology* Cloning, Molecular Fenitrothion / toxicity Glutathione Transferase / chemistry* Humans Lethal Dose 50 Molecular Sequence Data Phylogeny Sequence Alignment
IF 2.897
Times Cited 46
Silkworms EST database