INSILICO CHARACTERIZATION OF GLUTATHIONE S-TRANSFERASES AND THEIR INTERACTION STUDY IN MULBERRY SILKWORM, BOMBYX MORI

The Glutathione S-transferases are cytosolic enzymes that are found in both prokaryotes and eukaryotes. The GST multigene family are phase II detoxification enzymes that mainly helps to detoxify the large range of xenobiotic compounds in many organisms. These enzymes play a major role in detoxification pathway along with their related genes. We characterized the each GSTs class of silkworm such as Delta, Epsilon, Omega, Theta, Zeta and the phylogentic tree of GSTs were consructed. Further, we identified the conserved domains of GSTs such as thioredoxin_like and GST_C_family superfamily. Also, the G-site, H-site and dimer inferace of GSTs were identified. Around 10 conserved motifs were found by analyzing all GSTs of the silkworm. The silkworm genome sequences were mapped into the kegg pathway database and found the silkworm genes that are found in the xenobiotics metabolism pathway. Additionally, 128 protein-protein interactions of silkworm were found from the GSTs and their related genes of metabolic pathways. Further, functional enrichment analysis was shown. This study paves ways to understand the phase II detoxification enzymes, glutathione S-transferases and xenobiotics detoxification metabolic pathway of the mulberry silkworm.