Literature summary for 2.7.4.6 extracted from

Ishibashi, M.; Sakashita, K.; Tokunaga, H.; Arakawa, T.; Tokunaga, M.
Activation of halophilic nucleoside diphosphate kinase by a non-ionic osmolyte, trimethylamine N-oxide (2003), J. Protein Chem., 22, 345-351.

Activating Compound

Activating Compound	Comment	Organism	Structure
Trimethylamine N-oxide	concentration of 4 M required for activity, at pH 8 inclusion of low concentrations of NaCl required for activation	Halobacterium salinarum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
KCl	concentration of 3 M required for activity	Halobacterium salinarum
NaCl	concentration of 2 M required for activity	Halobacterium salinarum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + NDP	Halobacterium salinarum	contributes to the maintenance of the cellular pools of all nucleosides triphosphates	ADP + NTP	-	?
ATP + NDP	Halobacterium salinarum 4R	contributes to the maintenance of the cellular pools of all nucleosides triphosphates	ADP + NTP	-	?

Organism

Organism	UniProt	Comment	Textmining
Halobacterium salinarum	-	-	-
Halobacterium salinarum 4R	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Halobacterium salinarum

Renatured (Commentary)

Renatured (Comment)	Organism
extremely halophilic enzyme inactivated at low salt concentrations using heat-treatment or 6 M urea, addition of or dialysis against 2 M NaCl, 3 M KCl, or 4 M trimethylamine N-oxide required for effective refolding of enzyme, refolding using 4 M trimethylamine N-oxide is strongly pH-dependent, good refolding at pH 7, almost no activity regained at pH 8, at pH 8 inclusion of low concentrations of NaCl supports refolding and activation of activity	Halobacterium salinarum

Renatured (Comment)

Organism

extremely halophilic enzyme inactivated at low salt concentrations using heat-treatment or 6 M urea, addition of or dialysis against 2 M NaCl, 3 M KCl, or 4 M trimethylamine N-oxide required for effective refolding of enzyme, refolding using 4 M trimethylamine N-oxide is strongly pH-dependent, good refolding at pH 7, almost no activity regained at pH 8, at pH 8 inclusion of low concentrations of NaCl supports refolding and activation of activity

Halobacterium salinarum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + NDP	-	Halobacterium salinarum	ADP + NTP	-	?
ATP + NDP	contributes to the maintenance of the cellular pools of all nucleosides triphosphates	Halobacterium salinarum	ADP + NTP	-	?
ATP + NDP	-	Halobacterium salinarum 4R	ADP + NTP	-	?
ATP + NDP	contributes to the maintenance of the cellular pools of all nucleosides triphosphates	Halobacterium salinarum 4R	ADP + NTP	-	?