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Literature summary for 1.2.1.9 extracted from
- Engineering the allosteric properties of archaeal non-phosphorylating glyceraldehyde-3-phosphate dehydrogenases (2014), Biochim. Biophys. Acta, 1844, 759-766.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| D-glucose 1-phosphate | activates. Activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity | Sulfurisphaera tokodaii |  |
| D-glucose 1-phosphate | activates. Activation follows an increase in maximum velocity rather than in affinity glyceraldehyde-3-phosphate | Saccharolobus solfataricus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharolobus solfataricus |
| expression in Escherichia coli | Sulfurisphaera tokodaii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E141D | kcat for D-glyceraldehyde 3-phosphate is 2.1fold lower than wild-type value | Sulfurisphaera tokodaii |
| K137E | kcat for D-glyceraldehyde 3-phosphate is 1.1fold lower than wild-type value | Sulfurisphaera tokodaii |
| L138T | kcat for D-glyceraldehyde 3-phosphate is 1.3fold lower than wild-type value | Sulfurisphaera tokodaii |
| additional information | in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior | Sulfurisphaera tokodaii |
| additional information | in non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus tokodaii, D-glucose 1-phosphate-induced activation follows an increase in affinity for glyceraldehyde-3-phosphate rather than an increase in maximum velocity, whereas in the enzyme from Sulfolobus solfataricus, D-glucose 1-phosphate-induced activation follows an increase in maximum velocity rather than in affinity for glyceraldehyde-3-phosphate. To explore the molecular basis of this difference 14 mutants and 2 chimeras are generated. The analyses of chimeric enzymes generated from regions of the Sulfolobus tokodaii enzyme and the Sulfolobus solfataricus enzyme indicates that a 57-residue module located in the subunit interface is involved in their allosteric behavior | Saccharolobus solfataricus |
| R136K | kcat for D-glyceraldehyde 3-phosphate is 2.8fold lower than wild-type value | Sulfurisphaera tokodaii |
| Y139R | kcat for D-glyceraldehyde 3-phosphate is 302fold lower than wild-type value. The mutant enzyme no longer displays a sigmoidal K-type-like allostery but instead has apparent V-type allostery similar to that of the Sulfolobus solfataricus enzyme, suggesting that the residue located in the center of the homotetramer critically contributes to the allosteric behavior | Sulfurisphaera tokodaii |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 55000 | - |
4 * 55000, SDS-PAGE | Sulfurisphaera tokodaii |
| 57000 | - |
4 * 57000, SDS-PAGE | Saccharolobus solfataricus |
| 223000 | - |
gel filtration | Sulfurisphaera tokodaii |
| 230000 | - |
gel filtration | Saccharolobus solfataricus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | Q97U30 | - |
- |
| Saccharolobus solfataricus P2 | Q97U30 | - |
- |
| Sulfurisphaera tokodaii | Q96XP0 | - |
- |
| Sulfurisphaera tokodaii 7 | Q96XP0 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Saccharolobus solfataricus |
- |
Sulfurisphaera tokodaii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + NADP+ + H2O | - |
Sulfurisphaera tokodaii | 3-phospho-D-glycerate + NADPH + 2 H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + NADP+ + H2O | - |
Saccharolobus solfataricus | 3-phospho-D-glycerate + NADPH + 2 H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + NADP+ + H2O | - |
Sulfurisphaera tokodaii 7 | 3-phospho-D-glycerate + NADPH + 2 H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + NADP+ + H2O | - |
Saccharolobus solfataricus P2 | 3-phospho-D-glycerate + NADPH + 2 H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 55000, SDS-PAGE | Sulfurisphaera tokodaii |
| homotetramer | 4 * 57000, SDS-PAGE | Saccharolobus solfataricus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GAPN | - |
Sulfurisphaera tokodaii |
| GAPN | - |
Saccharolobus solfataricus |
| non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase | - |
Sulfurisphaera tokodaii |
| non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase | - |
Saccharolobus solfataricus |
| SSO3194 | locus name | Saccharolobus solfataricus |
| STK_24770 | locus name | Sulfurisphaera tokodaii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
assay at | Saccharolobus solfataricus |
| 60 | - |
assay at | Sulfurisphaera tokodaii |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.13 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 60°C, mutant enzyme Y139R | Sulfurisphaera tokodaii | |
| 15 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 60°C | Saccharolobus solfataricus | |
| 117 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 60°C, mutant enzyme R136K | Sulfurisphaera tokodaii | |
| 161 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 60°C, mutant enzyme E141D | Sulfurisphaera tokodaii | |
| 257 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 60°C, mutant enzyme L138T | Sulfurisphaera tokodaii | |
| 297 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 60°C, mutant enzyme K137E | Sulfurisphaera tokodaii | |
| 341 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 60°C, wild-type enzyme | Sulfurisphaera tokodaii | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Sulfurisphaera tokodaii |
| 8 | - |
assay at | Saccharolobus solfataricus |
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