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Substrate and thiol specificity of a stress‐inducible glutathione transferase from soybean
Author(s) -
Skipsey Mark,
Andrews Christopher J,
Townson Jane K,
Jepson Ian,
Edwards Robert
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00554-1
Subject(s) - glutathione , thiol , glutathione s transferase , biochemistry , chemistry , xenobiotic , peroxidase , enzyme , clone (java method) , substrate (aquarium) , gpx3 , glutathione reductase , glutathione peroxidase , biology , gene , ecology
An RT‐PCR‐derived clone encoding a stress‐inducible glutathione transferase (GST Gm 1) from soybean has been over‐expressed in E. coli . The enzyme was active as the dimer GST Gm 1‐1 and showed GST and glutathione peroxidase activity toward diverse xenobiotics, including analogues of natural stress‐metabolites. The selective herbicides, fomesafen and acifluorfen, were conjugated more actively with homoglutathione (hGSH), the major thiol in soybean, than with glutathione (GSH). No thiol preference was shown with the related herbicide, fluorodifen, while GSH was preferred with metolachlor and most non‐herbicide substrates. Similar thiol‐dependent specificities were observed in GST preparations from plants of varying GSH/hGSH content.