Molecular cloning, expression and enzymatic characterization of glutathione S-transferase from Antarctic sea-ice bacteria Pseudoalteromonas sp. ANT506.

@article{Shi2014MolecularCE,
  title={Molecular cloning, expression and enzymatic characterization of glutathione S-transferase from Antarctic sea-ice bacteria Pseudoalteromonas sp. ANT506.},
  author={Yonglei Shi and Quanfu Wang and Yanhua Hou and Yanyan Hong and Xiao Han and Jiali Yi and Junjie Qu and Yi Jun Lu},
  journal={Microbiological research},
  year={2014},
  volume={169 2-3},
  pages={179-84}
}
A glutathione S-transferase (GST) gene from Antarctic sea-ice bacteria Pseudoalteromonas sp. ANT506 (namely PsGST), was cloned and expressed in Escherichia coli. The open reading frame of PsGST comprised 654 bp encoding a protein of 217 amino acids with a calculated molecular size of 24.3 kDa. The rPsGST possesses the conserved amino acid defining the binding sites of glutathione (G-site) and substrate binding pocket (H-site) in GST N_3 family. PsGST was expressed in E. coli and the recombinant… CONTINUE READING
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