A cytosolic glutathione s-tranferase from Acidovorax sp. KKS102, a biphenyl/polychlorobiphenyl degrading organism is recently known to have a dehalogenation function on various organochlorine substrates. However, little is known about the specific amino acids involved in its structural stability and catalytic process. The in silico site-directed mutagenesis of a highly conserved region, Ala154, Asp155 and Tyr157 in the C-terminal domain of the cytosolic glutathione s-transferase from Acidovorax sp. was carried out using Deep View/Swiss-Pdb Viewer molecular graphics program for all the proteinogenic amino acids. The amino acid substitutions in this region directly affected the theoretical 3D model of the transferase protein entity through alteration of the predicted stabilization forces which may in turn affect the structural stability and perhaps the activity of the enzyme
