Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Geobacillus thermodenitrificans |
Protein Variants | Comment | Organism |
---|---|---|
T353A | mutation of the N-terminal residue of the 21 kDa subunit, abolishes the post-translational cleavage of the pro-enzyme, but does not completely block the hydrolytic action | Geobacillus thermodenitrificans |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
21000 | - |
2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer | Geobacillus thermodenitrificans |
40000 | - |
2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer | Geobacillus thermodenitrificans |
103000 | - |
gel filtration | Geobacillus thermodenitrificans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus thermodenitrificans | - |
- |
- |
Geobacillus thermodenitrificans NG80-2 | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | the enzyme is synthesized as a precursor homotetrameric protein of 60-kDa per subunit, and undergoes an internal post-translational cleavage of the 60 kDa monomer into 40- and 21-kDa shorter subunits, which are then assembled into an active heterotetramer composed of two 40- and two 21-kDa subunits | Geobacillus thermodenitrificans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glutathione + H2O | L-glutamate is transferred to H2O, c.f. EC 3.4.19.9 | Geobacillus thermodenitrificans | L-cysteinylglycine + L-glutamate | - |
? | |
glutathione + H2O | L-glutamate is transferred to H2O, c.f. EC 3.4.19.9 | Geobacillus thermodenitrificans NG80-2 | L-cysteinylglycine + L-glutamate | - |
? | |
additional information | enzyme does not show any transpeptidase activity | Geobacillus thermodenitrificans | ? | - |
? | |
additional information | enzyme does not show any transpeptidase activity | Geobacillus thermodenitrificans NG80-2 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | 2 * 40000 + 2 * 21000, SDS-PAGE. The unprocessed enzyme forms an already active homotetramer, whereas the mature enzyme is a fully active compact alpha2beta2-heterotetramer | Geobacillus thermodenitrificans |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
52 | - |
- |
Geobacillus thermodenitrificans |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
24 h, 83% residual activity | Geobacillus thermodenitrificans |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.8 | - |
- |
Geobacillus thermodenitrificans |