Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.1.1 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)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Pyrococcus horikoshii
-
strain OT3
-
Pyrococcus horikoshii OT-3
-
strain OT3
-

Purification (Commentary)

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

Synonyms

Synonyms Comment Organism
inorganic pyrophosphatase
-
Pyrococcus horikoshii
PPase
-
Pyrococcus horikoshii