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Literature summary for 3.6.1.5 extracted from
- The crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 represents a conformational intermediate in the reductive activation mechanism of the tetrameric enzyme (2013), Proteins, 81, 1271-1276.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli Rosetta pLysS cells | Toxoplasma gondii |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop vapor diffusion method, using 100 mM Tris pH 8.5, 50 mM MgCl2, 25% (v/v) pentaerythritol propoxylate | Toxoplasma gondii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Toxoplasma gondii | Q27895 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| anion exchange column chromatography and gel filtration | Toxoplasma gondii |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | - |
Toxoplasma gondii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NTPDase1 | - |
Toxoplasma gondii |
| nucleoside triphosphate diphosphohydrolase 1 | - |
Toxoplasma gondii |
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Release 2023.1 (January 2023)
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