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Literature summary extracted from
- Crystal structure of recombinant triosephosphate isomerase from Bacillus stearotherophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions (1995), Protein Sci., 4, 2594-2604.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.3.1.1 | triosephosphate isomerase complexed with the competitive inhibitor 2-phosphoglycolate, at 2.8 A resolution | Geobacillus stearothermophilus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.3.1.1 | Phosphoglycolate | 2-phosphoglycolate | Geobacillus stearothermophilus |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.3.1.1 | Geobacillus stearothermophilus | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.3.1.1 | D-Glyceraldehyde 3-phosphate | - |
Geobacillus stearothermophilus | Glycerone phosphate | - |
? | |
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Release 2023.1 (January 2023)
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