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Literature summary for 2.7.4.6 extracted from

  • Ishibashi, M.; Uchino, M.; Arai, S.; Kuroki, R.; Arakawa, T.; Tokunaga, M.
    Reduction of salt-requirement of halophilic nucleoside diphosphate kinase by engineering S-S bond (2012), Arch. Biochem. Biophys., 525, 47-52.
    View publication on PubMed
Search for more literature for 2.7.4.6

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
D148C the mutation enhances stability and folding in low salt solution by S-S bond. The mutant shows increased thermal stability by about 10°C in 0.2 M NaCl over the wild type enzyme Halobacterium salinarum

Organism

Organism UniProt Comment Textmining
Halobacterium salinarum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HisTrap column chromatography and Hitrap Q column chromatography Halobacterium salinarum

Renatured (Commentary)

Renatured (Comment) Organism
refolding of heat-denatured wild type enzyme in 50 mM Tris-HCl (pH 7.5) occurs depending on the salt concentration. Refolding rate is slow even in the presence of 2 M NaCl, reaching maximum at 2 days Halobacterium salinarum

Subunits

Subunits Comment Organism
hexamer native enzyme Halobacterium salinarum

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 80 after 5 min incubation, the wild type enzyme loses about 30% activity at 30°C and 100% activity at 40°C in 0.2 M NaCl. In 3.8 M NaCl, the wild type enzyme remains stable up to 75°C and then rapidly loses activity at 80°C Halobacterium salinarum