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Structural modelling and molecular characterization of omega‐class glutathione S ‐transferase 2 from D rosophila melanogaster
Author(s) -
Kim K.,
Yim J.
Publication year - 2014
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12086
Subject(s) - glutathione s transferase , gene isoform , homology modeling , homology (biology) , isozyme , drosophila melanogaster , enzyme , biology , glutathione , biochemistry , amino acid , gene
Glutathione S ‐transferase omega ( GSTO ) is a recently identified Glutathione S ‐transferase ( GST) , and it has several known functions and variable distribution patterns in many organisms. In D rosophila , GstO2 exists as two isoforms, GstO2A and GstO2B . Despite the high sequence homology between the two GstO2 isoforms, they have different physiological functions. In the present study, we characterized the structural and molecular properties of D rosophila melanogaster GstO2 isoforms. Homology modelling of GstO2 s using I ‐ TASSER servers for protein structure and function prediction revealed that the two GstO2 s have different electropotential surface distributions and different shapes of the substrate‐binding sites. The recombinant GstO2 s have native molecular weights of ∼60 kDa. GstO2 s have similar optimum conditions for enzymatic reactions at pH 8.0 and 40 °C. The kinetic parameters of the reduction of dehydroascorbate by these two GstO2 s were determined. Collectively, our results provide structural insights into the different substrate profiles of the GstO2 isoforms.