A mu-class glutathione S-transferase from the marine shrimp Litopenaeus vannamei: molecular cloning and active-site structural modeling.

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. (c) 2004 Wiley Periodicals, Inc.