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Literature summary for 2.7.4.6 extracted from

  • Ishibashi, M.; Arakawa, T.; Tokunaga, M.
    Facilitated folding and subunit assembly in Escherichia coli and in vitro of nucleoside diphosphate kinase from extremely halophilic archaeon conferred by amino-terminal extension containing hexa-His-tag (2004), FEBS Lett., 570, 87-92.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
fusion of extra sequence containing hexa-His-tag at amino-terminus of the enzyme facilitates folding and activation in Escherichia coli Halobacterium salinarum

General Stability

General Stability Organism
amino-terminal extension enhances dimer to hexamer assembly and stabilizes the structure in low salt Halobacterium salinarum

Organism

Organism UniProt Comment Textmining
Halobacterium salinarum P61136
-
-
Halobacterium salinarum JCM 11081 P61136
-
-

Renatured (Commentary)

Renatured (Comment) Organism
refolding of the His-tagged enzyme after denaturation is much more efficient than refolding of the untagged enzyme Halobacterium salinarum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
340
-
pH 8.0, temperature not specified in the publication Halobacterium salinarum

Subunits

Subunits Comment Organism
dimer folded His-tagged enzyme isolated from Escherichia coli forms a hexamer in both 0.2 M and 3.8 M NaCl at 30 °C, while the native enzyme purified from Halobacterium salinarum dissociates to dimer in 0.2 M NaCl Halobacterium salinarum
hexamer folded His-tagged enzyme isolated from Escherichia coli forms a hexamer in both 0.2 M and 3.8 M NaCl at 30 °C, while the native enzyme purified from Halobacterium salinarum dissociates to dimer in 0.2 M NaCl Halobacterium salinarum

Synonyms

Synonyms Comment Organism
HsNDK
-
Halobacterium salinarum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Halobacterium salinarum