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Literature summary extracted from

  • Liu, B.; Li, X.; Gao, R.; Zhou, W.; Xie, G.; Bartlam, M.; Pang, H.; Feng, Y.; Rao, Z.
    Crystallization and preliminary X-ray analysis of inorganic pyrophosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 (2004), Acta Crystallogr. Sect. D, 60, 577-579.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.1 expression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.1 purified recombinant enzyme, hanging drop vapour diffusion method, 20 mg/ml protein in 5 mM Tris-HCl, pH 8.0, and 50 mM NaCl, 18°C, 0.001 ml versus 0.001 ml reservoir solution containing 8% PEG 4000, 0.1 M sodium acetate, pH 4.5, for needle-shaped crystals, and 3.8% PEG 4000, 0.1 M sodium acetate, pH 5.0-5.2, for large crystals, X-ray diffraction structure determination and analysis at 2.7 A resolution Pyrococcus horikoshii

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.1 Pyrococcus horikoshii
-
strain OT3
-
3.6.1.1 Pyrococcus horikoshii OT-3
-
strain OT3
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.1 recombinant enzyme from Escherichia coli Pyrococcus horikoshii

Synonyms

EC Number Synonyms Comment Organism
3.6.1.1 inorganic pyrophosphatase
-
Pyrococcus horikoshii
3.6.1.1 PPase
-
Pyrococcus horikoshii