EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.2.1.107 | H176N | the mutant shows a Km value 5times smaller than for the wild type enzyme while the Km value for arsenate is about 5times larger. The mutant has a significantly reduced thermal stability at 65°C. The half-life for thermal denaturation for the mutant holoenzyme is increased nearly 100fold over the corresponding value for the apoenzyme | Geobacillus stearothermophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.107 | D-glyceraldehyde 3-phosphate + arsenate + NAD+ | Geobacillus stearothermophilus | - |
1-arsono-3-phospho-D-glycerate + NADH + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.107 | Geobacillus stearothermophilus | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.107 | D-glyceraldehyde 3-phosphate + arsenate + NAD+ | - |
Geobacillus stearothermophilus | 1-arsono-3-phospho-D-glycerate + NADH + H+ | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.107 | GPD | - |
Geobacillus stearothermophilus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.2.1.107 | 100 | - |
D-glyceraldehyde 3-phosphate | mutant enzyme H176N, at pH 8.5 and 27°C | Geobacillus stearothermophilus | |
1.2.1.107 | 100 | - |
D-glyceraldehyde 3-phosphate | wild type enzyme, at pH 8.5 and 27°C | Geobacillus stearothermophilus |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.107 | NAD+ | - |
Geobacillus stearothermophilus |