Substrate and thiol specificity of a stress‐inducible glutathione transferase from soybean

FEBS Letters

Townson, Jane K¹  Jepson, Ian¹  Skipsey, Mark²  Edwards, Robert¹  Andrews, Christopher J² 

[1] Zeneca Agrochemicals, Jealott's Hill Research Station, Bracknell, RG42 6ET, UK;Department of Biological Sciences, University of Durham, Durham DH1 3LE, UK

关键词: Glutathione transferase;    Herbicides;    Glutathione;    Glutathione peroxidase;    Homoglutathione;    (Glycine max);    CDNB;    1-chloro-2;    4-dinitrobenzene;    DTT;    dithiothreitol;    GSH;    glutathione;    GST;    glutathione transferase;    hGSH;    homoglutathione;    SDS-PAGE;    sodium dodecyl sulphate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(97)00554-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

An RT-PCR-derived clone encoding a stress-inducible glutathione transferase (GSTGm1) from soybean has been over-expressed in E. coli. The enzyme was active as the dimer GSTGm1-1 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.

【 授权许可】

Unknown