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Literature summary for 2.7.4.6 extracted from

  • Ishibashi, M.; Ida, K.; Tatsuda, S.; Arakawa, T.; Tokunaga, M.
    Interaction of hexa-His tag with acidic amino acids results in facilitated refolding of halophilic nucleoside diphosphate kinase (2011), Int. J. Biol. Macromol., 49, 778-783.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Star (DE3) cells Halobacterium salinarum

Protein Variants

Protein Variants Comment Organism
D112S the mutant shows reduced specific activity compared to the wild type enzyme Halobacterium salinarum
D58G the mutant shows strongly reduced specific activity compared to the wild type enzyme Halobacterium salinarum
D58G/D63G the mutant shows no refolding enhancement and strongly reduced specific activity compared to the wild type enzyme Halobacterium salinarum
D63G the mutant shows slightly reduced specific activity compared to the wild type enzyme Halobacterium salinarum
G114D the mutant, which forms a dimer in low salt solution, is strongly stabilized by His-tag to form a stable hexamer and shows strongly reduced specific activity compared to the wild type enzyme Halobacterium salinarum

Organism

Organism UniProt Comment Textmining
Halobacterium salinarum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ATP-agarose column chromatography, and gel filtration Halobacterium salinarum

Renatured (Commentary)

Renatured (Comment) Organism
in 50 mM Tris-HCl buffer containing 3 M NaCl, at 4°C. Refolding is extremely slow, reaching the nearly full activity at 72 h Halobacterium salinarum

Synonyms

Synonyms Comment Organism
NDK
-
Halobacterium salinarum
nucleoside diphosphate kinase
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Halobacterium salinarum

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
90
-
heating at 90°C for 5 min is sufficient to fully inactivate the protein Halobacterium salinarum