Literature summary for 2.7.4.1 extracted from

Nocek, B.; Kochinyan, S.; Proudfoot, M.; Brown, G.; Evdokimova, E.; Osipiuk, J.; Edwards, A.M.; Savchenko, A.; Joachimiak, A.; Yakunin, A.F.
Polyphosphate-dependent synthesis of ATP and ADP by the family-2 polyphosphate kinases in bacteria (2008), Proc. Natl. Acad. Sci. USA, 105, 17730-17735.

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli strains BL21 (DE3) and B834 (DE3)	Pseudomonas aeruginosa
expressed in Escherichia coli strains BL21 (DE3) and B834 (DE3)	Sinorhizobium meliloti

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 7.5), 0.1 M Na-formate, 0.1 M Li-sulfate, and 0.3 M NDSB 211	Sinorhizobium meliloti
hanging drop vapor diffusion method, using 0.1 M HEPES-K (pH 7.0), 5% tacsimate, and 10% PEG MME 5K	Pseudomonas aeruginosa

Protein Variants

Protein Variants	Comment	Organism
D148A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
D223A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
D307A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
D320A	the mutant shows reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
D323A	the mutant shows reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
D362A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
D437A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
D93A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
E304A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
E90A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
K311A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
K473A	the mutant shows reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
K97A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
Q202A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
Q416A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
R149A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
R205A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
R209A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
R263A	the mutant shows almost wild type activity	Sinorhizobium meliloti
R316A	the mutant shows reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
R325A	the mutant shows reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
R363A	the mutant shows almost no activity compared to the wild type enzyme	Pseudomonas aeruginosa
R419A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
R423A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
R477A	the mutant shows increased activity compared to the wild type enzyme	Pseudomonas aeruginosa
W194A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
W408A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa
Y233A	the mutant shows strongly reduced activity compared to the wild type enzyme	Sinorhizobium meliloti
Y447A	the mutant shows strongly reduced activity compared to the wild type enzyme	Pseudomonas aeruginosa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	no activity in the absence of a divalent metal cation, Mg2+ is the most effective metal, whereas low activity is observed with Co2+ or Ni2+ and no activity is observed in the presence of Mn2+ or Ca2+	Pseudomonas aeruginosa
Mg2+	no activity in the absence of a divalent metal cation, Mg2+ is the most effective metal, whereas low activity is observed with Co2+ or Ni2+ and no activity is observed in the presence of Mn2+ or Ca2+	Sinorhizobium meliloti

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
97000	-	gel filtration	Pseudomonas aeruginosa
124500	-	gel filtration	Sinorhizobium meliloti

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	-	-	-
Sinorhizobium meliloti	Q92SA6	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pseudomonas aeruginosa
-	Sinorhizobium meliloti

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ATP + (phosphate)n	-	Pseudomonas aeruginosa	ADP + (phosphate)n+1	-	?
ATP + (phosphate)n	-	Sinorhizobium meliloti	ADP + (phosphate)n+1	-	?
additional information	PA3455 protein is also active with (phosphate)3 as a phosphodonor, but its activity and substrate affinity are lower than those with (phosphate)12-13	Pseudomonas aeruginosa	?	-	?

Subunits

Subunits	Comment	Organism
homodimer	x-ray crystallography	Pseudomonas aeruginosa
homotetramer	x-ray crystallography	Sinorhizobium meliloti

Synonyms

Synonyms	Comment	Organism
family-2 polyphosphate kinase	-	Pseudomonas aeruginosa
family-2 polyphosphate kinase	-	Sinorhizobium meliloti
PA3455 protein	-	Pseudomonas aeruginosa
PPK2	-	Pseudomonas aeruginosa
PPK2	-	Sinorhizobium meliloti
SMc02148 protein	-	Sinorhizobium meliloti

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	9.5	-	Pseudomonas aeruginosa
8	9.5	-	Sinorhizobium meliloti

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Pseudomonas aeruginosa
ATP	-	Sinorhizobium meliloti