Elham Kazemi - Department of Biology, Faculty of Sciences, Maraghe University
Sasan Mohsenzadeh - Department of Biology, Faculty of Sciences, Shiraz University, Shiraz

Glutathione S-transferase is a family of multifunctional detoxification enzymes which are mainly cytosolic that detoxify natural and exogenous toxic compounds by conjugation with glutathione. Glutathione, an endogenous tripeptide, is important as either a reducing agent or a nucleophilic scavenger. This moleculealleviates the chemical toxicity in plants by reaction of glutathione S-transferase, and its conjugates can be transported to vacuole or apoplast. The plant soluble glutathione S-transferases grouped today into five distinct Phi, Tau, Zeta, Theta, lambda classes. Many glutathione S-transferase have been purifiedfrom animals over the last ۳۰ years and classified by their biochemical and immunological characteristics.Sequencing studies were used to extend this system. In this article four bread wheat (Triticum aestivum L.) Iranian cultivar glutathione S-transferase partial gene sequence and one bacterium (Sphingomonas paucimobilis) strain glutathione S-transferase partial gene sequence from NCBI database were comparedby nucleotide alignment using multalin software and with distance in evaluation showed ۴۳.۴% nucleotide similarity. Databases have allowed us to classify glutathione S-transferase and study their evolution and sequence diversity, while crystallographic studies have provided powerful insights into their structuralbiology.

GST, Sphingomonas paucimobilis, Iranian wheat cultivar, bacterium, Evaluation