EC Number   |
General Information |
Reference |
|---|
  1.8.5.7 | evolution |
Xi class glutathione transferases (GSTs) are a group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are widely distributed in bacteria, fungi, and plants but not in higher eukaryotes. Xi class GSTs are also frequently found in archaea. Multiple alignment analysis of NmGHR in comparison with other Xi class GSTs show that all sequences display several common motifs. All members exhibit a strictly conserved CPWA motif that could play a key role in the binding of GS-(hydro)-quinones. Phylogenetic analysis, members of prokaryotic and eukaryotic Xi class GSTs and their homologous belonging to different GST classes are characterized by the presence of a cysteine residue in the G-site, overview |
-, 764737 |
| 1.8.5.7 | more |
enzyme NmGHR displays is enriched in negatively charged residues, which are evenly distributed along the surface of the protein, and is characterized by a peculiar distribution of hydrophobic residues. The thiol binding site (G-site) of the enzyme is well suited for hosting gamma-glutamyl-cysteine. Circular dichroism analysis of NmGHR |
-, 764737 |
| 1.8.5.7 | physiological function |
the disruption of PcpF in makes the mutant lose the glutathionyl-hydroquinone lyase activities in the cell extracts. The mutant becomes more sensitive to pentachlorophenol toxicity and has a significantly decreased pentachlorophenol degradation rate |
-, 740614 |
