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Literature summary for 2.3.2.2 extracted from
- Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: An enzyme specialized in hydrolase activity (2010), Biochimie, 92, 464-474.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Geobacillus thermodenitrificans |
Protein Variants
| 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 [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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Geobacillus thermodenitrificans | - |
- |
- |
| Geobacillus thermodenitrificans NG80-2 | - |
- |
- |
Posttranslational Modification
| 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 and Products (Substrate)
| 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
| 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 [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 52 | - |
- |
Geobacillus thermodenitrificans |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
24 h, 83% residual activity | Geobacillus thermodenitrificans |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
- |
Geobacillus thermodenitrificans |
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Release 2023.1 (January 2023)
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