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Literature summary for 3.6.1.66 extracted from
- Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3 functional significance of interprotomer conformational changes (2008), J. Mol. Biol., 375, 1013-1025 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| oil microbatch method. High resolution crystal structures of the enzyme in two unliganded forms and in three liganded forms with the substrate ITP, the product IMP and the divalent cation Mn2+ are determined. Based on these structures, a mechanism of the divalent cation-dependent ITP hydrolysis is proposed | Pyrococcus horikoshii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus horikoshii | O59580 | - |
- |
| Pyrococcus horikoshii OT-3 | O59580 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Pyrococcus horikoshii |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dITP/XTP pyrophosphatase | - |
Pyrococcus horikoshii |
| PH1917 | - |
Pyrococcus horikoshii |
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Release 2023.1 (January 2023)
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