Reference - Detail
| RRC ID | 12240 |
|---|---|
| Author | Yamamoto K, Teshiba S, Shigeoka Y, Aso Y, Banno Y, Fujiki T, Katakura Y. |
| Title | Characterization of an omega-class glutathione S-transferase in the stress response of the silkmoth. |
| Journal | Insect Mol Biol |
| Abstract |
The glutathione S-transferase (GST) superfamily is involved in detoxification of various xenobiotics. Using real-time PCR, mRNA encoding an omega-class GST of Bombyx mori (bmGSTO) was shown to be induced after exposure to various environmental stresses. A soluble form of recombinant protein (rbmGSTO) was functionally overexpressed in Escherichia coli cells and purified to homogeneity. Cys 38 and Pro 39 were found to be highly conserved in omega-class GSTs, and their roles were investigated by site-directed mutagenesis/kinetic analysis. Mutations of Cys 38 and Pro 39 residues affected the catalytic efficiency of enzymes, indicating that the presence of Cys 38 and Pro 39 residues is important for bmGSTO activity. Thus, bmGSTO could contribute to increasing the environmental stress resistance of lepidopteran insects. |
| Volume | 20(3) |
| Pages | 379-86 |
| Published | 2011-6-1 |
| DOI | 10.1111/j.1365-2583.2011.01073.x |
| PMID | 21435060 |
| MeSH | Amino Acid Sequence Animals Base Sequence Bombyx / enzymology Bombyx / genetics Bombyx / physiology* Cysteine / genetics Escherichia coli / genetics Fat Body / enzymology Glutathione Transferase / genetics Glutathione Transferase / metabolism* Hydrogen Peroxide / metabolism Molecular Sequence Data Mutagenesis, Site-Directed Mutation Oxidative Stress* Proline / genetics Recombinant Proteins / genetics Recombinant Proteins / metabolism Sequence Homology, Amino Acid Xenobiotics / metabolism |
| IF | 2.533 |
| Times Cited | 25 |
| WOS Category | ENTOMOLOGY BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Altmetric score |
オルトメトリクス指標項目
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| Total number of mentions | 0 |
| Resource | |
| Silkworms | silkmoth |