A mu-class glutathione S-transferase from the marine shrimp Litopenaeus vannamei: molecular cloning and active-site structural modeling
| Autor: | Citlalli Harris-Valle, Gloria Yepiz-Plascencia, Carmen A. Contreras-Vergara, Rogerio R. Sotelo-Mundo |
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| Rok vydání: | 2004 |
| Předmět: |
animal structures
Health Toxicology and Mutagenesis Molecular Sequence Data Molecular cloning Toxicology Biochemistry Complementary DNA Animals Humans Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Conserved Sequence DNA Primers Glutathione Transferase Binding Sites biology Base Sequence Sequence Homology Amino Acid cDNA library fungi General Medicine biology.organism_classification Molecular biology Shrimp Glutathione S-transferase Prawn biology.protein Molecular Medicine Hepatopancreas Anostraca Sequence Alignment |
| Zdroj: | Journal of biochemical and molecular toxicology. 18(5) |
| ISSN: | 1095-6670 |
| Popis: | A cDNA clone coding for a mu-class glutathione S-transferase (GST) was isolated from a hepatopancreas cDNA library from the shrimp Litopenaeus vannamei. The deduced amino acid sequence (215 amino acids) has >50% identity to rodents and other mammals mu-class GSTs. Using RT-PCR, the shrimp GST transcript was detected in hepatopancreas, hemocytes, gills, and muscle, but not in pleopods. The shrimp GST sequence was computer modeled and found to fit the classical two-domain GST structure. Domain I, containing the glutathione (GSH) binding site, is more conserved compared to the flexible C-terminal domain II. Residue Q208 appears to be a key to substrate specificity by comparison with mammalian GST mutants. This position is commonly occupied by serine or threonine in mammalian mu-class GSTs, and shrimp Q208 may affect the affinity to substrates like aminochrome or 1,3-dimethyl-2-cyano-1-nitrosoguanidine. This is the first report of molecular cloning and structural modeling of a crustacean GST and provides new insights into the nature of the detoxification response on marine invertebrates. |
| Databáze: | OpenAIRE |
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