Cloned (Comment) | Organism |
---|---|
gene yghU, expression in Escherichia coli strain BL21(DE3), expression of the selenomethionine YghU derivative in Escherichia coli strain B834 DE3 | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
purified recombinant YghU, hanging-drop vapor diffusion method, YghU at 20 mg/ml in 30 mM NaH2PO4, pH 7.0, 1 mM DTT, and 20 mM GSH, is mixed with an equal volume of reservoir solution containing 0.1 M Bis-Tris, 0.2 M NaCl, pH 5.5, 25% w/v PEG 3350, 25°C, 1 week, X-ray diffraction structure determination and analysis at 1.5-2.5 A resolution | Escherichia coli |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
oxidized glutathione | - |
Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
gene yghU | - |
Purification (Comment) | Organism |
---|---|
recombinant YghU from strain BL21(DE3) by anion and cation exchange chromatography and dialysis | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-chloro-2,4-dinitrobenzene + glutathione | - |
Escherichia coli | S-(2,4-dinitrophenyl)glutathione + HCl | - |
? | |
additional information | YghU from Escherichia coli binds two molecules of GSH in each active site. YghU exhibits little or no GSH transferase activity with most typical electrophilic substrates but does possess a modest catalytic activity toward several organic hydroperoxides. The enzyme also exhibits disulfide-bond reductase activity towards 2-hydroxyethyl disulfide | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GSH transferase homologue | - |
Escherichia coli |
nu-class glutathione transferase | - |
Escherichia coli |
YghU | - |
Escherichia coli |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Escherichia coli |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | 7 | assay at | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | structures and properties of YghU and YfcG indicate that they are members of the same distinct subfamily of GSH transferase homologues, proposed to be called the Nu-class GSH transferases. Cytoscape cluster analysis of the GSH transferase superfamily, overvew | Escherichia coli |