Crystallization (Comment) | Organism |
---|---|
binary complex structure with glutathionyl-menadione. The structure reveals a large H-site that could accommodate various substituted hydroquinones and a hydrogen network of three Tyr residues that could provide the proton for reductive deglutathionylation | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
C63A | catalytic residue, mutant displays negligible activity | Escherichia coli |
Y195F | catalytic residue, mutant displays negligible activity | Escherichia coli |
Y253F | catalytic residue, mutant displays negligible activity | Escherichia coli |
Y296F | catalytic residue, mutant displays negligible activity | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.34 | - |
2-(glutathione-S-yl)-hydroquinone | wild-type, pH 7.5, temperature not specified in the publication | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P42620 | - |
- |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.16 | - |
mutant Y253F, pH 7.5, temperature not specified in the publication | Escherichia coli |
0.19 | - |
mutant Y195F, pH 7.5, temperature not specified in the publication | Escherichia coli |
0.4 | - |
mutant Y296F, pH 7.5, temperature not specified in the publication | Escherichia coli |
8.65 | - |
wild-type, pH 7.5, temperature not specified in the publication | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glutathione + 2-(glutathione-S-yl)-hydroquinone | - |
Escherichia coli | glutathione disulfide + hydroquinone | - |
? |
Synonyms | Comment | Organism |
---|---|---|
glutathionyl-hydroquinone reductase | - |
Escherichia coli |
yqjG | - |
Escherichia coli |