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ADP + (phosphate)20
ATP + (phosphate)19
-
-
-
-
r
ADP + (phosphate)3
ATP + (phosphate)2
ADP + (phosphate)45
ATP + (phosphate)44
ADP + (phosphate)46
ATP + (phosphate)45
ADP + (phosphate)60
ATP + (phosphate)59
ADP + (phosphate)65
ATP + (phosphate)64
ADP + (phosphate)66
ATP + (phosphate)65
ADP + (phosphate)n
ATP + (phosphate)n-1
ADP + (phosphate)n+1
ATP + (phosphate)n
ADP + hexametaphosphate
ATP + ?
ADP + phosphate(6)
ATP + phosphate(5)
ANU33171.1
i.e. hexametaphosphate
-
-
?
ADP + polyphosphate(4)
ATP + polyphosphate(3)
ADP + polyphosphate25
ATP + polyphosphate24
-
-
-
-
?
ADP + polyphosphate65
ATP + polyphosphate64
-
-
-
-
?
AMP + (phosphate)60
ADP + (phosphate)59
AMP + (phosphate)60
ATP + (phosphate)58
AMP + (phosphate)n+1
ADP + (phosphate)n
AMP + (phosphate)n+2
ATP + (phosphate)n
ATP + (phosphate)45
ADP + (phosphate)46
ATP + (phosphate)65
ADP + (phosphate)66
ATP + (phosphate)n
ADP + (phosphate)n+1
ATP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
r
ATP + ATP
ADP + (phosphate)n+1
-
polyP not required as primer
-
-
r
ATP + phosphate
ADP + diphosphate
CDP + (phosphate)n
CTP + (phosphate)n-1
CDP + (phosphate)n+1
CTP + (phosphate)n
dADP + (phosphate)20
dATP + (phosphate)19
-
-
-
-
r
dADP + (phosphate)n+1
dATP + (phosphate)n
dAMP + (phosphate)n+1
dADP + (phosphate)n
dCDP + (phosphate)n+1
dCTP + (phosphate)n
-
-
-
ir
dGDP + (phosphate)n+1
dGTP + (phosphate)n
-
-
-
ir
GDP + (phosphate)20
GTP + (phosphate)19
-
isoform PPK1 affinity for the ADP as a substrate is about 70fold high as opposed to GDP
-
-
r
GDP + (phosphate)n
GTP + (phosphate)n-1
GDP + (phosphate)n+1
GTP + (phosphate)n
GDP + (phosphate)n+2
guanosine 5'-tetraphosphate + (phosphate)n
GMP + (phosphate)n+1
GDP + (phosphate)n
GTP + (phosphate)65
GDP + (phosphate)66
-
-
-
-
?
GTP + (phosphate)n
GDP + (phosphate)n+1
GTP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
r
ITP + (phosphate)n
IDP + (phosphate)n+1
TDP + (phosphate)n+1
TTP + (phosphate)n
-
-
-
ir
UDP + (phosphate)20
UTP + (phosphate)19
-
-
-
-
r
UDP + (phosphate)n
UTP + (phosphate)n-1
UDP + (phosphate)n+1
UTP + (phosphate)n
[phosphate](n+1) + ADP
[phosphate](n) + ATP
additional information
?
-
ADP + (phosphate)3
ATP + (phosphate)2
the enzyme can utilize short chain polyphosphates, PolyP3 as the phosphate donor, however, its activity increases in the presence of long chain polyphosphates PolyP17 or PolyP45
-
-
?
ADP + (phosphate)3
ATP + (phosphate)2
-
the enzyme can utilize short chain polyphosphates, PolyP3 as the phosphate donor, however, its activity increases in the presence of long chain polyphosphates PolyP17 or PolyP45
-
-
?
ADP + (phosphate)3
ATP + (phosphate)2
the enzyme can utilize short chain polyphosphates, PolyP3 as the phosphate donor, however, its activity increases in the presence of long chain polyphosphates PolyP17 or PolyP45
-
-
?
ADP + (phosphate)45
ATP + (phosphate)44
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)45
ATP + (phosphate)44
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)45
ATP + (phosphate)44
-
-
-
-
r
ADP + (phosphate)46
ATP + (phosphate)45
-
-
-
r
ADP + (phosphate)46
ATP + (phosphate)45
-
-
-
r
ADP + (phosphate)60
ATP + (phosphate)59
-
-
-
r
ADP + (phosphate)60
ATP + (phosphate)59
-
-
-
r
ADP + (phosphate)60
ATP + (phosphate)59
-
-
-
r
ADP + (phosphate)65
ATP + (phosphate)64
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)65
ATP + (phosphate)64
-
similar catalytic activities with either (phosphate)65 or (phosphate)45. Isoform PPK2 catalyzes polyphosphate-dependent phosphorylation of ADP to ATP at a rate 838times higher than the rate of polyphosphate synthesis
-
-
r
ADP + (phosphate)65
ATP + (phosphate)64
-
-
-
-
r
ADP + (phosphate)66
ATP + (phosphate)65
-
-
-
r
ADP + (phosphate)66
ATP + (phosphate)65
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
Thermosynechococcus vestitus
not (phosphate)3, (phosphate)4 as preferred phosphate donor
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
polyphosphate kinase directly or indirectly regulates DNA polymerase activity or fidelity
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
Francisella tularensis Schu 4
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?, r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
the enzyme preferentially catalyzes the long-chain polyP hexametaphosphate as the phosphate donor. No activity with AMP. No formation of ATP in the presence of pyrophosphate or tripolyphosphate
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
the enzyme preferentially catalyzes the long-chain polyP hexametaphosphate as the phosphate donor. No activity with AMP. No formation of ATP in the presence of pyrophosphate or tripolyphosphate
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme prefers polyphosphate of 25 to 50 in chain length
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme prefers polyphosphate of 25 to 50 in chain length
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
the enzyme can utilize short chain polyphosphates, PolyP3 as the phosphate donor, however, its activity increases in the presence of long chain polyphosphates PolyP17 or PolyP45
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
the enzyme can utilize short chain polyphosphates, PolyP3 as the phosphate donor, however, its activity increases in the presence of long chain polyphosphates PolyP17 or PolyP45
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
the enzyme can utilize short chain polyphosphates, PolyP3 as the phosphate donor, however, its activity increases in the presence of long chain polyphosphates PolyP17 or PolyP45
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
substrates are polyphosphates or hexametaphosphate
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
no activity with GDP, diphosphate or tripolyphosphate
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
the enzyme preferentially catalyzes the long-chain polyP hexametaphosphate as the phosphate donor. No activity with AMP
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
the enzyme preferentially catalyzes the long-chain polyP hexametaphosphate as the phosphate donor. No activity with AMP
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
no activity with AMP
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
the enzyme protects Salmonella enterica from weak organic acid stress. Polyphosphate may acts as a chemical chaperone that helps refold homoserine transsuccinylase and/or may stimulate proteolysis of toxic denatured protein. The instability of homoserine transsuccinylase may provide a metabolic fuse that blocks growth under conditions that denature proteins. The sensitivity of this fuse is modulated by polyphosphate
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ADP + hexametaphosphate
ATP + ?
-
-
-
?
ADP + hexametaphosphate
ATP + ?
-
-
-
?
ADP + polyphosphate(4)
ATP + polyphosphate(3)
-
-
-
-
?
ADP + polyphosphate(4)
ATP + polyphosphate(3)
mutant enzyme H102K/A106E/V115T exhibits the capability to utilize polyP(4) as phosphate donor to synthesize ATP. The wild-type enzyme shows no activity with polyphosphate(4)
-
-
?
AMP + (phosphate)60
ADP + (phosphate)59
-
-
-
r
AMP + (phosphate)60
ADP + (phosphate)59
-
-
-
r
AMP + (phosphate)60
ADP + (phosphate)59
-
-
-
r
AMP + (phosphate)60
ATP + (phosphate)58
-
-
-
r
AMP + (phosphate)60
ATP + (phosphate)58
-
-
-
r
AMP + (phosphate)60
ATP + (phosphate)58
-
-
-
r
AMP + (phosphate)n+1
?
-
-
-
?
AMP + (phosphate)n+1
?
-
-
-
?
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
?
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
?
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
?
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
?
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+1
ADP + (phosphate)n
Francisella tularensis Schu 4
-
-
-
r
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
?
AMP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
?
AMP + (phosphate)n+2
ATP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+2
ATP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+2
ATP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+2
ATP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+2
ATP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+2
ATP + (phosphate)n
-
-
-
r
ATP + (phosphate)45
ADP + (phosphate)46
-
-
-
-
r
ATP + (phosphate)45
ADP + (phosphate)46
-
-
-
r
ATP + (phosphate)45
ADP + (phosphate)46
-
-
-
r
ATP + (phosphate)45
ADP + (phosphate)46
-
-
-
-
r
ATP + (phosphate)65
ADP + (phosphate)66
-
-
-
-
r
ATP + (phosphate)65
ADP + (phosphate)66
-
-
-
r
ATP + (phosphate)65
ADP + (phosphate)66
-
-
-
r
ATP + (phosphate)65
ADP + (phosphate)66
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
Achromobacter butyri
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no activity with CTP, GTP and TTP
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
Chlamydomonas sp.
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125 and prefers the polyphosphate synthesis reaction direction
polyphosphate product chain length determination by NMR spectroscopy
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125 and prefers the polyphosphate synthesis reaction direction
polyphosphate product chain length determination by NMR spectroscopy
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
DdPPK1 products are heterogeneous in chain length, with broad-range chain lengths of 50-300 Pi residues, and shorter compared to those of Escherichia coli
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
PPK1 is the principal enzyme responsible for reversible synthesis of polyphosphate from the terminal phosphate of ATP
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
polyphosphate chains of lenths of 700-800 residues
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
via phosphorylated enzyme intermediate
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
best substrates are polyphosphates with more than 132 residues
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no activity with phosphates of 5 residues or below
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no primer substrate required
via phosphorylated enzyme intermediate
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
incorporates gamma-phosphate of ATP into long-chain polyphosphate molecules
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
polyphosphate kinase may be involved in nucleotide metabolism
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
involved in phosphate metabolism of bacteria
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
essential role of the enzyme during the initial steps of colonisation of the mouse gastric mucosa. The enzyme may act on the virulence of Helicobacter pylori partly through an energy dependent mechanism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis. GTP and GDP are not recognized as substrates
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
autophosphorylation, i.e. the gamma-phosphate of ATP becomes covalently attached to the enzyme under condition of polyphosphate synthesis, 0.52-0.92 mol phosphate per mol enzyme
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Oryza sativa Japonica Group cv. Wuyugeng 7
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
strictly processive mechanism of polyphosphate elongation, phosphate or short-chains of polyphosphates serve as primers, majority of the synthesized polyphosphates is 750 residues long
polyphosphate as primer: product with 750 residues, phosphate as primer: product with 300-2000 residues, i.e. major form with chain length of 2000
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Q9S646
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate kinase 1 and 2
polyphosphate with 200-800 residues
?
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate kinase 1 and 2
poyphosphate with 500-800 residues
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
essential for biofilm development, quorum sensing, and virulence of Pseudomonas aeruginosa
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK1 is essential for a successful ocular infection by the organism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
very slow reverse reaction
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
no activity with AMP
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
enzyme synthesizes polyphosphates of 300000-400000 Da
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + (phosphate)n
ADP + (phosphate)n+1
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
incorporates gamma-phosphate of ATP into long-chain polyphosphate molecules
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
glycogen-bound polyphosphate kinase
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
the enzyme does not require the presence of histones for its activity
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Thermosynechococcus vestitus
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
ir
ATP + phosphate
ADP + diphosphate
-
-
-
-
r
ATP + phosphate
ADP + diphosphate
-
-
-
-
r
ATP + phosphate
ADP + diphosphate
-
-
-
-
?
CDP + (phosphate)n
CTP + (phosphate)n-1
-
-
-
?
CDP + (phosphate)n
CTP + (phosphate)n-1
-
-
-
?
CDP + (phosphate)n+1
CTP + (phosphate)n
-
-
-
ir
CDP + (phosphate)n+1
CTP + (phosphate)n
-
-
-
ir
CDP + (phosphate)n+1
CTP + (phosphate)n
-
the efficiency of polyphosphate utilization by PKK3 is 100%
-
-
?
dADP + (phosphate)n+1
dATP + (phosphate)n
-
-
-
?
dADP + (phosphate)n+1
dATP + (phosphate)n
-
-
-
?
dADP + (phosphate)n+1
dATP + (phosphate)n
-
-
-
ir
dADP + (phosphate)n+1
dATP + (phosphate)n
-
-
-
?
dADP + (phosphate)n+1
dATP + (phosphate)n
-
-
-
?
dAMP + (phosphate)n+1
dADP + (phosphate)n
-
-
-
?
dAMP + (phosphate)n+1
dADP + (phosphate)n
-
-
-
?
dAMP + (phosphate)n+1
dADP + (phosphate)n
-
-
-
?
dAMP + (phosphate)n+1
dADP + (phosphate)n
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
r
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
efficiency of NDP substrates in descending order: ADP, dADP, dGDP, GDP, TDP, UDP, CDP, dCDP
-
ir
GDP + (phosphate)n+1
GTP + (phosphate)n
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
PPK2 catalyses the synthesis of GTP from GDP using polyphosphate rather than ATP as phosphate donor, PPK2 preferentially synthesizes GTP over CTP or UTP in vitro
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
10times higher activity than Escherichia coli polyphosphate kinase
-
ir
GDP + (phosphate)n+1
GTP + (phosphate)n
-
chains of 30-50 residues are optimal, chains of 15-700 residues can also serve. GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
chains of 30-50 residues are optimal, chains of 15-700 residues can also serve. GDP is preferred over ADP over nucleoside diphosphate acceptors
-
-
?
GDP + (phosphate)n+2
guanosine 5'-tetraphosphate + (phosphate)n
-
-
-
?
GDP + (phosphate)n+2
guanosine 5'-tetraphosphate + (phosphate)n
-
diphosphate group transfer
-
ir
GMP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
?
GMP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
?
GMP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
?
GMP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
?
GTP + (phosphate)n
GDP + (phosphate)n+1
-
-
-
-
r
GTP + (phosphate)n
GDP + (phosphate)n+1
-
lower activity compared to ATP
-
-
r
GTP + (phosphate)n
GDP + (phosphate)n+1
polyphosphate kinase 2
-
?
ITP + (phosphate)n
IDP + (phosphate)n+1
-
-
-
-
r
ITP + (phosphate)n
IDP + (phosphate)n+1
-
lower activity compared to ATP
-
-
r
UDP + (phosphate)n
UTP + (phosphate)n-1
-
-
-
?
UDP + (phosphate)n
UTP + (phosphate)n-1
-
-
-
?
UDP + (phosphate)n+1
UTP + (phosphate)n
-
-
-
ir
UDP + (phosphate)n+1
UTP + (phosphate)n
-
-
-
ir
[phosphate](n+1) + ADP
[phosphate](n) + ATP
-
-
-
?
[phosphate](n+1) + ADP
[phosphate](n) + ATP
-
-
-
?
[phosphate](n+1) + ADP
[phosphate](n) + ATP
-
-
-
?
additional information
?
-
enzyme additionally displays adenylate kinase activity in both reaction directions
-
-
-
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
-
PKK2B also shows NDP kinase activity
-
-
?
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
-
PKK2B also shows NDP kinase activity
-
-
?
additional information
?
-
enzyme catalyzes the phosphorylation of AMP and GMP into ATP and GTP
-
-
-
additional information
?
-
enzyme catalyzes the phosphorylation of AMP and GMP into ATP and GTP
-
-
-
additional information
?
-
enzyme catalyzes the phosphorylation of AMP and GMP into ATP and GTP through step-by-step phosphorylation but also by pyrophosphorylation
-
-
-
additional information
?
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
the enzyme from Dictyostelium discoideum performs autophosphorylation and has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
-
-
?
additional information
?
-
-
the enzyme from Dictyostelium discoideum performs autophosphorylation and has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
-
-
?
additional information
?
-
enzyme additionally displays adenylate kinase activity in both reaction directions
-
-
-
additional information
?
-
Francisella tularensis Schu 4
enzyme additionally displays adenylate kinase activity in both reaction directions
-
-
-
additional information
?
-
the substrate specificity of FtPPK2 includes purine but not pyrimidine nucleotides. No activity with UDP and CDP as substrates. No formation of ADP or GDP from AMP or GMP
-
-
?
additional information
?
-
enzyme also accepts GDP, reaction of Ec 2.7.4.34. No substrates: CDP, UDP
-
-
-
additional information
?
-
enzyme preferentially accepts hexametaphosphate as the phosphate donor. No substrates: diphosphate or triphosphate, and AMP
-
-
-
additional information
?
-
-
enzyme preferentially accepts hexametaphosphate as the phosphate donor. No substrates: diphosphate or triphosphate, and AMP
-
-
-
additional information
?
-
enzyme preferentially accepts hexametaphosphate as the phosphate donor. No substrates: diphosphate or triphosphate, and AMP
-
-
-
additional information
?
-
-
maximum PPK activity is observed for wild-type AG83 Leishmania donovani amastigotes when ADP is the phosphate group acceptor from polyphosphate, the activity is 29 times higher than with GDP as phosphate group acceptor from polyphosphate. When AMP is the phosphate group acceptor from polyphosphate, the activity of PPK is 97times less than with ADP, existence of both PPK1 and PPK2 activity is probable in Leishmania donovani amastigotes. ATP formation from AMP shows lowest activity
-
-
?
additional information
?
-
-
maximum PPK activity is observed for wild-type AG83 Leishmania donovani amastigotes when ADP is the phosphate group acceptor from polyphosphate, the activity is 29 times higher than with GDP as phosphate group acceptor from polyphosphate. When AMP is the phosphate group acceptor from polyphosphate, the activity of PPK is 97times less than with ADP, existence of both PPK1 and PPK2 activity is probable in Leishmania donovani amastigotes. ATP formation from AMP shows lowest activity
-
-
?
additional information
?
-
enzyme additionally displays adenylate kinase activity in both reaction directions
-
-
-
additional information
?
-
enzyme is able to use nucleoside diphosphates ADP, GDP, CDP, and UDP
-
-
-
additional information
?
-
enzyme additionally displays adenylate kinase activity in both reaction directions
-
-
-
additional information
?
-
enzyme is able to use nucleoside diphosphates ADP, GDP, CDP, and UDP
-
-
-
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
the enzyme is unable to use triphosphate or pentaphosphate as phosphate donors
-
-
?
additional information
?
-
-
the enzyme is unable to use triphosphate or pentaphosphate as phosphate donors
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
in the absence of polyP, the enzyme (Ppk1) generates ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzes the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity
-
-
-
additional information
?
-
-
in the absence of polyP, the enzyme (Ppk1) generates ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzes the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity
-
-
-
additional information
?
-
in the absence of polyP, the enzyme (Ppk1) generates ATP and AMP from ADP, and ADP from ATP and AMP, suggesting that the enzyme catalyzes the transfer of a phosphate group between ADP molecules yielding ATP and AMP, thus exhibiting adenylate kinase activity
-
-
-
additional information
?
-
enzyme preferentially accepts hexametaphosphate as the phosphate donor. No or poor substrates: diphosphate or triphosphate, and AMP
-
-
-
additional information
?
-
-
enzyme preferentially accepts hexametaphosphate as the phosphate donor. No or poor substrates: diphosphate or triphosphate, and AMP
-
-
-
additional information
?
-
enzyme preferentially accepts hexametaphosphate as the phosphate donor. No or poor substrates: diphosphate or triphosphate, and AMP
-
-
-
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
-
-
?
additional information
?
-
-
paPpx is an exopolyphosphatase (EC 3.6.1.11), and is also a polyphosphate:ADP phosphotransferase, and the active site is the same as that one involved in the hydrolase activity
-
-
-
additional information
?
-
GTP (reaction of EC 2.7.4.34) and ATP are equally active in polyphosphate synthesis
-
-
-
additional information
?
-
-
GTP (reaction of EC 2.7.4.34) and ATP are equally active in polyphosphate synthesis
-
-
-
additional information
?
-
GTP (reaction of EC 2.7.4.34) and ATP are equally active in polyphosphate synthesis
-
-
-
additional information
?
-
gene ppk regulates the transcription accumulation of the stationary-phase sigma factor RpoS encoded by the rpoS gene, overview
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
-
-
?
additional information
?
-
enzyme additionally displays adenylate kinase activity in both reaction directions
-
-
-
additional information
?
-
-
the enzyme PPK from Streptomyces lividans also exhibits weak phospholipase D activity, EC 3.1.4.4, hydrolysing phosphatidylcholine, quantification of [3H]phosphatidic acid released from [3H]PC-labeled ELT3 cell membranes from phospholipase D-deficient cells, overview
-
-
?
additional information
?
-
-
production of choline from hydrolysis of 1,2-dioleoyl-sn-glycero-3-phosphocholine in the presence of the Amplex Red reagent by enzyme PPK
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + (phosphate)n
ATP + (phosphate)n-1
ADP + (phosphate)n+1
ATP + (phosphate)n
ATP + (phosphate)n
ADP + (phosphate)n+1
CDP + (phosphate)n
CTP + (phosphate)n-1
CDP + (phosphate)n+1
CTP + (phosphate)n
dADP + (phosphate)n+1
dATP + (phosphate)n
-
-
-
ir
dCDP + (phosphate)n+1
dCTP + (phosphate)n
-
-
-
ir
dGDP + (phosphate)n+1
dGTP + (phosphate)n
-
-
-
ir
GDP + (phosphate)n
GTP + (phosphate)n-1
GDP + (phosphate)n+1
GTP + (phosphate)n
TDP + (phosphate)n+1
TTP + (phosphate)n
-
-
-
ir
UDP + (phosphate)n
UTP + (phosphate)n-1
UDP + (phosphate)n+1
UTP + (phosphate)n
additional information
?
-
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
?
ADP + (phosphate)n
ATP + (phosphate)n-1
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
-
polyphosphate kinase directly or indirectly regulates DNA polymerase activity or fidelity
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzed ATP formation
-
-
r
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
enzyme is involved in polyphosphate synthesis. The polyphosphate kinase gene is transcribed from a sigma(E) dependent promoter, which could be responsive to environmental stresses
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
-
the enzyme protects Salmonella enterica from weak organic acid stress. Polyphosphate may acts as a chemical chaperone that helps refold homoserine transsuccinylase and/or may stimulate proteolysis of toxic denatured protein. The instability of homoserine transsuccinylase may provide a metabolic fuse that blocks growth under conditions that denature proteins. The sensitivity of this fuse is modulated by polyphosphate
-
-
?
ADP + (phosphate)n+1
ATP + (phosphate)n
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate utilization and accumulation contribute significantly to Campylobacter jejuni pathogenesis and affect its ability to adapt to specific stresses and stringencies
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
PPK1 is the principal enzyme responsible for reversible synthesis of polyphosphate from the terminal phosphate of ATP
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
polyphosphate kinase may be involved in nucleotide metabolism
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
involved in phosphate metabolism of bacteria
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
essential role of the enzyme during the initial steps of colonisation of the mouse gastric mucosa. The enzyme may act on the virulence of Helicobacter pylori partly through an energy dependent mechanism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
when Ppk1 from Myxococcus xanthus is incubated with 0.2 mM polyP60-70 and 1 mM ATP or ADP, the rate of ATP synthesis is approximately 1.5-fold higher than that of polyP synthesis. If in the same reaction the proportion of ADP in the ATP/ADP mixture exceeds one-third, the equilibrium shifts to ATP synthesis, suggesting that the enzyme preferentially catalyzes ATP formation
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Oryza sativa Japonica Group cv. Wuyugeng 7
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
Q9S646
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
PPK1 is essential for a successful ocular infection by the organism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Thermosynechococcus vestitus
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
CDP + (phosphate)n
CTP + (phosphate)n-1
-
-
-
?
CDP + (phosphate)n
CTP + (phosphate)n-1
-
-
-
?
CDP + (phosphate)n+1
CTP + (phosphate)n
-
-
-
ir
CDP + (phosphate)n+1
CTP + (phosphate)n
-
-
-
ir
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
efficiency of NDP substrates in descending order: ADP, dADP, dGDP, GDP, TDP, UDP, CDP, dCDP
-
ir
GDP + (phosphate)n+1
GTP + (phosphate)n
-
10times higher activity than Escherichia coli polyphosphate kinase
-
ir
UDP + (phosphate)n
UTP + (phosphate)n-1
-
-
-
?
UDP + (phosphate)n
UTP + (phosphate)n-1
-
-
-
?
UDP + (phosphate)n+1
UTP + (phosphate)n
-
-
-
ir
UDP + (phosphate)n+1
UTP + (phosphate)n
-
-
-
ir
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
-
accumulation of high levels of cytosolic phosphorus in the form of polyphosphate involving classII polyphosphate kinase isozymes, granular poly P, i.e. volutin, can make up to 37% of the internal cell volume, overview
-
-
?
additional information
?
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
-
the organism also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
-
-
?
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium tuberculosis, overview
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
?
additional information
?
-
-
polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria, mprAB-sigE-rel signalling cascade, overview. PPK1 is required for the stringent response, under conditions of stress polyP acts as a preferred donor for MprB-mediated phosphorylation of MprA facilitating transcription of the sigE gene thereby leading finally to the enhancement of the transcription of rel in Mycobacterium smegmatis, overview
-
-
?
additional information
?
-
gene ppk regulates the transcription accumulation of the stationary-phase sigma factor RpoS encoded by the rpoS gene, overview
-
-
?
additional information
?
-
-
the enzyme PPK from Streptomyces lividans also exhibits weak phospholipase D activity, EC 3.1.4.4, hydrolysing phosphatidylcholine, quantification of [3H]phosphatidic acid released from [3H]PC-labeled ELT3 cell membranes from phospholipase D-deficient cells, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cs+
-
activates wild-type, full-length enzyme paPpx(1-506)
NH4+
-
activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with NH4+ is sigmoid and reaches its maximum activity at concentrations of 30 mM. Km(app)NH4+ is 10 mM
Rb+
-
activates wild-type, full-length enzyme paPpx(1-506)
Ca2+
partially active in the presence of 5 mM Ca2+, 25% compared to activity with 5 mM Mg2+
Ca2+
activates, best cation
Co2+
ANU33171.1
activates
Co2+
-
1.5-2.5fold lower activation than with Mg2+, inhibitory with Mg2+ as activator
Co2+
partially active in the presence of 5 mM Co2+, 23% compared to activity with 5 mM Mg2+
K+
-
a nonessential activator of paPpx, presence of K+ does not affect the affinity of the enzyme for Mg2+, activates wild-type, full-length enzyme paPpx(1-506). The activity curve obtained with K+ is sigmoid and reaches its maximum activity at concentrations of 80 mM. Km(app)K+ is 42 mM
KCl
Dictyostelium discoideum also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
Mg2+
-
maximal activity at 10 mM
Mg2+
-
maximal activation at 10 mM
Mg2+
ANU33171.1
activates
Mg2+
-
optimal at 10 mM, activates
Mg2+
-
required for activity
Mg2+
-
maximal activity at 12-13 mM
Mg2+
-
maximal activity at 10 mM
Mg2+
-
required for activity
Mg2+
-
maximal activity of polyphosphate synthesis, ATP and GTP synthesis, and guanosine 5'-tetraphosphate synthesis at 5.0, 2.0, 1.0 and 0.2 mM
Mg2+
-
maximal activity at 5-10 mM at 1 mM ATP
Mg2+
required, best at 10 mM
Mg2+
optimum concentration 10 mM
Mg2+
Mn2+ is preferred over Mg2+
Mg2+
-
necessary for activity
Mg2+
optimal above 0.5 mM
Mg2+
-
optimum activity at 30 mM Mg2+
Mg2+
-
optimum Mg2+ concentration is 5 mM
Mg2+
-
required for activity
Mg2+
-
maximal activity at 2 mM
Mg2+
the enzyme requires Mg2+ or Mn2+ for maximum activity. Optimal concentration for polyphosphate synthesis is between 1 and 2.5 mM
Mg2+
polyphosphate kinase 2, preferred in ATP synthesis over Mn2+
Mg2+
-
5fold higher activation than Mn2+, at optimal concentration of 10 mM
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+
Mg2+
preference for Mn2+ over Mg2+
Mg2+
-
required, values of Km(app)Mg2+ in paPpx(1-506) and NpaPpx(1-314) are 0.30 mM and 0.28 mM, respectively. The interaction between paPpx(1-506) and Mg2+ occurs in the N-terminal domain
Mg2+
Mg2+ is favored over Mn2+ by 5fold at optimal concentration of 10 mM
Mg2+
recombinant polyphosphate kinase, maximal activity at 10 mM
Mg2+
activates, best cation
Mg2+
-
required for activity
Mg2+
-
inhibitory above 6 mM
Mg2+
-
active substrate: MgATP
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+
Mg2+
-
50% as effective as Mn2+
Mg2+
Thermosynechococcus vestitus
-
Mg2+
Thermosynechococcus vestitus
optimal above 0.5 mM
Mn2+
-
can replace Mg2+ to some extent
Mn2+
ANU33171.1
activates
Mn2+
-
optimal at 10 mM, activates highly
Mn2+
-
activation, can replace Mg2+
Mn2+
-
1.5-2.5fold lower activation than with Mg2+
Mn2+
-
2 mM, 22% of activation with Mg2+
Mn2+
required, best at 1 mM
Mn2+
optimum concentration 1 mM
Mn2+
Mn2+ is preferred over Mg2+
Mn2+
-
necessary for activity
Mn2+
-
optimum activity at 1 mM Mn2+
Mn2+
-
activation, can replace Mg2+
Mn2+
the enzyme requires Mg2+ or Mn2+ for maximum activity. Optimal concentration for polyphosphate synthesis is 1 mM
Mn2+
polyphosphate kinase 2, 10 mM preferred in polyphosphate synthesis over Mg2+
Mn2+
-
Mg2+ shows 5fold higher activation than Mn2+, at optimal concentration of 10 mM
Mn2+
preference for Mn2+ over Mg2+
Mn2+
Mg2+ is favored over Mn2+ by 5fold at optimal concentration of 10 mM
Mn2+
activates, best cation
Mn2+
-
activation, can replace Mg2+
Mn2+
-
maximal activity at 1.0-2.0 mM, inhibition above 2 mM
Mn2+
-
active substrate: MnATP
Mn2+
-
maximal activity at 2 mM
Mn2+
-
stimulates, preferred metal ion
Zn2+
ANU33171.1
activates
Zn2+
-
activation, 0.4 mM, 10% as effective as Mg2+
Zn2+
partially active in the presence of 5 mM Zn2+, 21% compared to activity with 5 mM Mg2+
Zn2+
-
Zn2+ is able to activate the enzyme only 20% compared to Mg2+
additional information
-
not activated by Ca2+
additional information
-
not activated by Ca2+
additional information
lower optimal concentration for Mn2+ ions than Mg2+ ions
additional information
-
not activated by Na+ and polyphosphate
additional information
-
Fe2+, Zn2+, Cu2+ cannot be used by the enzyme
additional information
-
not activated by Ca2+
additional information
-
behavior of the full-length paPpx(1-506) and N-paPpx(1-314) against different concentration of divalent ions such as Mg2+, Zn2+, Ca2+, and Mn2+ as effectors, in presence of a saturating concentration (0.008 mM) for the substrate polyphosphate65. The activation of both enzyme variants by Mg2+ is similar and shows no inhibition at high concentrations of this ion. The activation by Ca2+ and Mn2+ is negligible. Li+ and Na+ have no effects on enzyme activity, while NH4+, K+, Rb+, and Cs+ are activators of paPpx(1-506). Tetramethylammonium is not an activator of paPpx(1-506)
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
not activated by NH4Cl
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2-anilinoethane-1,1-diyl)bis(phosphonic acid)
(2E)-2-[(4-nitrophenyl)methylidene]-4,4-diphosphonobutanoic acid
2-[2-amino-3-[(2-amino-3-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-3-oxopropyl)disulfanyl]propanamido]-3-(4-hydroxyphenyl)propanoic acid
treating the wild-type Escherichia coli with the inhibitor, at 0.050 mM, results in a metabolic fingerprint that is an almost identicalntical metabolic behavior to the ppk1 knockout mutant
6-(4-aminobenzamido)-5-[(E)-[1-(2-chloro-5-sulfophenyl)-5-hydroxy-3-methyl-1H-pyrazol-4-yl]diazenyl]naphthalene-2-sulfonic acid
treating the wild-type Escherichia coli with the inhibitor, at 0.050 mM, results in a metabolic fingerprint that is completely identical to that of ppk1 knockout mutant
ammonium hydrochloride
-
50% inhibition at 200 mM
Ca2+
-
1 mM, 10% inhibition
Cu2+
-
0.1 mM, 92% inhibition, 1 mM, complete inhibition
ellagic acid
Q9S646
ellagic acid derivatives from Terminalia chebula increase the susceptibility of Pseudomonas aeruginosa to stress by inhibiting polyphosphate kinase, oveview. Ellagic acid derivatives completely inhibit PPK1 activity at 0.5 mg/ml. Ellagic acid derivatives-treated Pseudomonas aeruginosa cells show marked reduction in polyphosphate granules in cytosol. Ellagic acid derivatives from Terminalia chebula inhibit PPK1 expression and its activity and increase the sensitivity of Pseudomonas aeruginosa to desiccation and oxidative stress while reducing tolerance to piperacillin
G-quadruplex thrombin binding aptamer
binds to PPK2 with a KD of 870 nM, noncompetitive
-
Guanidine HCl
-
5 mM, 50% inhibition of polyphosphate synthesis
guanosine 5'-tetraphosphate
histone
-
reverse reaction, strong, activates forward reaction in the presence of phosphate
hydrolyzed glycogen
-
complete inhibition
-
MnATP2-
-
at high concentrations, above 0.6 mM, activating below
NH4Cl
-
200 mM, approx. 50% inhibition of glycogen-bound polyphosphate kinase
NSC-30205
0.1 mM, inhibits more than 80%, cytotoxic to THP-1 macrophages with TC50 value 0.01 mM
-
NSC-345647
0.1 mM, inhibits more than 80%, cytotoxic to THP-1 macrophages with TC50 value 0.005 mM
-
NSC-35676
0.1 mM, inhibits more than 80%, non-cytotoxic to THP-1 cells even at 0.05 mM concentration
-
NSC-9037
0.1 mM, inhibits more than 80%, non-cytotoxic to THP-1 cells even at 0.05 mM concentration
-
phalloidin
a heptapeptide toxin from the mushroom Amanita phalloides, which binds tightly and specifically to polymerized actin, inhibits DdPPK2 and DdPPK1, the latter by 80% at 10 nM, the molar ratio of phalloidin to DdPPK1 of 10:15 results in complete inhibition of DdPPK1 activity
Sodium fluoride
-
slight inhibition
threonyltyrosyl-N-[(1R)-1-[(3-aminopropyl)amino]-2-(carboxyoxy)-2-oxoethyl]serinamide
poor chemical inhibitor of PPK1, it shows a drop of approximately 20% in the WT biofilm formation ability
Zn2+
-
0.1 mM, 67% inhibition, 1 mM, complete inhibition
[(2,3-dichloroanilino)methylene]bis(phosphonic acid)
-
[(3,5-dichloroanilino)methylene]bis(phosphonic acid)
-
[(3-aminoanilino)methylene]bis(phosphonic acid)
[(3-carbamimidamidoanilino)methylene]bis(phosphonic acid)
[(4-benzylanilino)methylene]bis(phosphonic acid)
-
[2-(2,3-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
[2-(3-chloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
[2-(3-nitroanilino)ethane-1,1-diyl]bis(phosphonic acid)
-
[2-[(1-amino-2-methylbutyl)(hydroxy)phosphoryl]ethyl]phosphonic acid
(2-anilinoethane-1,1-diyl)bis(phosphonic acid)
-
(2-anilinoethane-1,1-diyl)bis(phosphonic acid)
-
(2E)-2-[(4-nitrophenyl)methylidene]-4,4-diphosphonobutanoic acid
-
(2E)-2-[(4-nitrophenyl)methylidene]-4,4-diphosphonobutanoic acid
-
(NH4)2SO4
-
40 mM, almost complete inhibition
(NH4)2SO4
-
activation up to 100 mM; inhibition at higher concentrations; strong inhibition
(NH4)2SO4
-
strong inhibition
ADP
-
0.025 mM, 0.05 mM, 0.1 mM and 0.25 mM, 56%, 68%, 77% and 100% inhibition, respectively of polyphosphate synthesis in crude extracts
ADP
-
0.08 mM, complete inhibition
ADP
-
0.2 mM, complete inhibition
ADP
-
50%, 70% and 93% inhibition at 0.08 mM, 0.15 mM and 0.2 mM ADP, respectively
ADP
-
competitive inhibition
ADP
-
substrate inhibition
ADP
Q9S646
product inhibition
ADP
-
0.25 mM, approx. 50% inhibition, 1 mM, complete inhibition
ADP
-
4 mM, product inhibition
ADP
-
2 mM, 50% inhibition of glycogen-bound polyphosphate kinase; product inhibition, about 50% inhibition at 2 mM
AMP
-
-
AMP
-
at high concentrations
AMP
-
15% and 70% inhibition of the forward reaction at AMP/ADP ratios of 1 and 10, respectiverly
ATP
-
substrate inhibition, at high concentrations
ATP
-
free form, above 0.008 mM
ATP
-
20% substrate inhibition at 2.4 mM
Co2+
-
1 mM, 40% inhibition
Co2+
complete inhibition; complete inhibition; complete inhibition
diphosphate
-
weak inhibition
diphosphate
-
1 mM, complete inhibition
diphosphate
-
10 mM, 66% inhibition of polyphosphate synthesis, 75% inhibition of GTP synthesis
diphosphate
-
1 mM, complete inhibition
EDTA
complete inhibition
EDTA
-
10 mM, complete inhibition
EDTA
low inhibition; low inhibition
F-
-
5 mM, complete inhibition
F-
-
20 mM, complete inhibition
F-
-
5 mM, 75% inhibition
F-
-
10 mM, complete inhibition
F-
-
20 mM, complete inhibition
F-
-
2 mM, 25% inhibition of glycogen-bound polyphosphate kinase
GMP
-
-
GMP
-
competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
guanosine 5'-tetraphosphate
-
guanosine 5'-tetraphosphate
-
guanosine 5'-tetraphosphate
-
guanosine 5'-tetraphosphate
-
KCl
inhibits PPK1 80% at 500 mM, but not PPK2
KCl
-
50 mM, 50% inhibition
Mg2+
-
8 mM, complete inhibition
Mg2+
-
free form, above 6 mM, activating below
Mn2+
-
weak inhibition at 10 mM Mg2+
Mn2+
-
free form, above 2 mM, activating below
phosphate
-
above 20 mM; activates in the presence of histone
phosphate
-
5.5 mM and 11 mM, 33% and 49% inhibition of forward reaction
phosphate
-
2 mM, 50% inhibition of glycogen-bound polyphosphate kinase; strong inhibition
Polyphosphate
-
65 residues, competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
Polyphosphate
-
substrate inhibition at 2 mM
polyphosphate(4)
-
short polyphosphates inhibit the enzyme by blocking the ADP binding pocket
-
polyphosphate(4)
short polyphosphates inhibit the enzyme by blocking the ADP binding pocket
-
[(3-aminoanilino)methylene]bis(phosphonic acid)
-
[(3-aminoanilino)methylene]bis(phosphonic acid)
-
[(3-carbamimidamidoanilino)methylene]bis(phosphonic acid)
-
[(3-carbamimidamidoanilino)methylene]bis(phosphonic acid)
-
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-(3-chloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
-
[2-(3-chloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
-
[2-[(1-amino-2-methylbutyl)(hydroxy)phosphoryl]ethyl]phosphonic acid
-
[2-[(1-amino-2-methylbutyl)(hydroxy)phosphoryl]ethyl]phosphonic acid
-
additional information
-
no inhibition by UMP and CMP
-
additional information
-
not inhibited by NaCl
-
additional information
screening of low-molecular-weight organophosphorus inhibitors against polyphosphate kinases from Cytophaga hutchinsonii and Escherichia coli. For Cytophaga hutchinsonii PPK2, almost all active inhibitors belong to N-substituted alpha-aminobisphosphonic acids preferentially possessing an additional basic function
-
additional information
-
not inhibited by 2,4-dinitrophenol or potassium arsenate
-
additional information
-
not inhibited by 3',5'-adenosine monophosphate
-
additional information
-
MIC values of wild-type and mutant strain ExPEC for diverse antibiotics, i.e. beta-lactams cefotaxime, ceftazidime, ampicillin, cefazolin, tazobactam, and ticarcillin, glycopeptide vancomycin, aminoglycosides gentamicin, gentamicin sulfate, amikacin macrolide, erythromycin, quinolones norfloxacin and levofloxacin, sulfonamide trimethoprim, sulfadiazine nitrofurans macrodantin, and lipopeptde polymyxin B, overview. Biofilm-grown DELTAppk and wild-type cells are similarly tolerant and more tolerant than planktonic cells
-
additional information
screening of low-molecular-weight organophosphorus inhibitors against polyphosphate kinases from Cytophaga hutchinsonii and Escherichia coli. For Escherichia coli PPK1, only individual compounds with a distinct scaffold and functional group arrangement show potency
-
additional information
-
not inhibited by bafilomycin A1 or a protonophore
-
additional information
-
not inhibited by KCl; not inhibited by NaCl; not inhibited by phosphate; not inhibited by polyphosphate
-
additional information
-
a G9-quadruplex DNA aptamer inhibits isoform PPK2 with an IC50 of 40 nM and exhibits noncompetitive inhibition kinetics
-
additional information
-
enzymatic hydrolysis of glycogen
-
additional information
-
a G9-quadruplex DNA aptamer inhibits isoform PPK2 with an IC50 of 105 nM and exhibits noncompetitive inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.005 - 0.006
(phosphate)45
-
0.0063
(phosphate)46
pH 8.5, temperature not specified in the publication
-
0.0054 - 0.0063
(phosphate)65
-
0.006
(phosphate)66
pH 8.5, temperature not specified in the publication
-
0.011 - 0.29
(phosphate)n+1
29.39
Hexametaphosphate
pH 8.0, 30°C
1.67
phosphate
-
pH 7.0, 30°C
15.2 - 19
polyphosphate(4)
-
0.00311 - 0.00336
polyphosphate25
0.00249 - 0.00311
polyphosphate65
-
3.6
UDP
pH 8.0, 30°C, recombinant isozyme PPK2-3
additional information
additional information
-
0.005
(phosphate)45
pH 8.5, temperature not specified in the publication
-
0.005
(phosphate)45
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
0.006
(phosphate)45
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
0.0054
(phosphate)65
pH 8.5, temperature not specified in the publication
-
0.0054
(phosphate)65
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
0.0063
(phosphate)65
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
0.011
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
0.013
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
0.29
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
0.03
ADP
-
pH 8.0, 30°C, wild-type enzyme
0.033
ADP
wild-type enzyme, pH and temperature not specified in the publication
0.075
ADP
mutant enzyme N121D, pH and temperature not specified in the publication
0.1
ADP
-
in 50 mM Tris-HCl pH-7.5, 10 mM NH4SO4,10 mM KPO4, pH 7.0, 4 mM MgCl2, 50 mM NaCl, at 37°C
0.16
ADP
-
isoform PPK1, pH and temperature not specified in the publication
0.176
ADP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
0.18
ADP
-
pH 6.5-8.5, 25°C
0.18
ADP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
0.2
ADP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
0.246
ADP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.358
ADP
mutant N121D, pH not specified in the publication, temperature not specified in the publication
0.38
ADP
pH 8.5, temperature not specified in the publication
0.38
ADP
-
50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
0.546
ADP
wild-type, pH not specified in the publication, temperature not specified in the publication
2
ADP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
2.3
ADP
pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T
2.47
ADP
mutant D62A, pH not specified in the publication, temperature not specified in the publication
2.47
ADP
mutant enzyme D62A, pH and temperature not specified in the publication
2.5
ADP
pH 8.0, 30°C, recombinant isozyme PPK2-2
3.21
ADP
mutant D192A, pH not specified in the publication, temperature not specified in the publication
3.21
ADP
mutant enzyme D192A, pH and temperature not specified in the publication
3.25
ADP
mutant enzyme R178A, pH and temperature not specified in the publication
3.25
ADP
mutant R178A, pH not specified in the publication, temperature not specified in the publication
4.03
ADP
mutant D117N, pH not specified in the publication, temperature not specified in the publication
4.03
ADP
mutant enzyme D117N, pH and temperature not specified in the publication
6.18
ADP
mutant enzyme R118A, pH and temperature not specified in the publication
6.18
ADP
mutant R118A, pH not specified in the publication, temperature not specified in the publication
6.8
ADP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
8
ADP
-
isoform PPK2, pH and temperature not specified in the publication
9.546
ADP
wild-type enzyme, pH and temperature not specified in the publication
12.3
ADP
mutant enzyme K66A, pH and temperature not specified in the publication
12.3
ADP
mutant K66A, pH not specified in the publication, temperature not specified in the publication
0.033
AMP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.075
AMP
mutant N121D, pH not specified in the publication, temperature not specified in the publication
0.246
AMP
wild-type enzyme, pH and temperature not specified in the publication
0.358
AMP
mutant enzyme N121D, pH and temperature not specified in the publication
0.075
ATP
-
pH 7.0, 75°C
0.075
ATP
-
pH 7.0, 75°C, glycogen-complexed enzyme
0.17
ATP
-
pH 7.2, 30°C, recombinant wild-type enzyme
0.33
ATP
pH 8.5, temperature not specified in the publication
0.33
ATP
-
50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
0.53
ATP
-
ATP in form of MnATP2-
0.8
ATP
-
in 50 mM Tris-HCl pH-7.5, 10 mM NH4SO4,10 mM KPO4, pH 7.0, 4 mM MgCl2, 50 mM NaCl, at 37°C
0.83
ATP
-
pH 7.0, 20°C, polyphosphate kinase activity in cell extracts, detrmined with Robinson and Wood method
1.18
ATP
-
pH 7.0, 20°C, polyphosphate kinase activity in cell extracts, kinetic analysis
1.2
ATP
pH 7.2, room temperature, recombinant polyphosphate kinase
1.35
ATP
-
isoform PPK1, pH and temperature not specified in the publication
1.38
ATP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
1.47
ATP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
1.5 - 2
ATP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
2.06
ATP
pH 7.5, 37°C, mutant enzyme D230N
2.07
ATP
pH 7.5, 37°C, wild-type enzyme
2.08
ATP
pH 7.5, 37°C, mutant enzyme E245K
5.2
ATP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
13
ATP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
0.11
dADP
pH 8.0, 30°C
0.71
dAMP
pH 8.0, 30°C
0.16
GDP
-
pH 7.5, 37°C, guanosine 5'-tetraphosphate synthesis
1.2
GDP
pH 8.0, 30°C, recombinant isozyme PPK2-1
11.3
GDP
-
isoform PPK1, pH and temperature not specified in the publication
2.88
GMP
pH 8.0, 30°C
0.14
GTP
-
-
0.14
GTP
-
pH 7.2, 30°C, recombinant wild-type enzyme
0.66
GTP
-
50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
1
ITP
-
-
1
ITP
-
pH 7.2, 30°C, recombinant wild-type enzyme
0.035
Polyphosphate
-
pH 7.5, 37°C, guanosine 5'-tetraphosphate synthesis
15
Polyphosphate
-
pH 7.2, 30°C, recombinant wild-type enzyme
15.2
polyphosphate(4)
-
pH 8.0, 30°C, wild-type enzyme
-
19
polyphosphate(4)
pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T
-
0.00311
polyphosphate25
-
pH 8.0, 37°C, full-length enzyme
0.00336
polyphosphate25
-
pH 8.0, 37°C, truncated enzyme
0.00249
polyphosphate65
-
pH 8.0, 37°C, full-length enzyme
-
0.00311
polyphosphate65
-
pH 8.0, 37°C, truncated enzyme
-
additional information
additional information
-
exponential kinetics
-
additional information
additional information
Michalis-Menten steady state kinetic analysis of FtPPK2 substrate specificity, overview
-
additional information
additional information
-
kinetic analysis of recombinant wild-type and truncated mutant enzymes, polyphosphatase activity (EC 3.6.1.11) and polyphosphate:ADP phosphotransferase activity, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.02 - 50
(phosphate)45
-
53
(phosphate)46
pH 8.5, temperature not specified in the publication
-
0.02 - 53
(phosphate)65
-
50
(phosphate)66
pH 8.5, temperature not specified in the publication
-
5.53 - 132
(phosphate)n+1
43
ITP
-
pH 7.2, 30°C, recombinant wild-type enzyme
5.6 - 15
polyphosphate(4)
-
0.31 - 4.28
polyphosphate25
0.29 - 3.93
polyphosphate65
-
0.02
(phosphate)45
pH 8.5, temperature not specified in the publication
-
0.02
(phosphate)45
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
50
(phosphate)45
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
0.02
(phosphate)65
pH 8.5, temperature not specified in the publication
-
0.02
(phosphate)65
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
53
(phosphate)65
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
5.53
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
29.63
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
132
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
0.0015
ADP
mutant D192A, pH not specified in the publication, temperature not specified in the publication
0.0022
ADP
mutant R118A, pH not specified in the publication, temperature not specified in the publication
0.0031
ADP
mutant R178A, pH not specified in the publication, temperature not specified in the publication
0.0053
ADP
mutant K66A, pH not specified in the publication, temperature not specified in the publication
0.015
ADP
mutant N121D, pH not specified in the publication, temperature not specified in the publication
0.016
ADP
mutant D62A, pH not specified in the publication, temperature not specified in the publication
0.032
ADP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.072
ADP
mutant D117N, pH not specified in the publication, temperature not specified in the publication
0.15
ADP
mutant enzyme D192A, pH and temperature not specified in the publication
0.22
ADP
mutant enzyme R118A, pH and temperature not specified in the publication
0.246
ADP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.31
ADP
mutant enzyme R178A, pH and temperature not specified in the publication
0.53
ADP
mutant enzyme K66A, pH and temperature not specified in the publication
1.59
ADP
mutant enzyme D62A, pH and temperature not specified in the publication
2.9
ADP
pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T
5.22
ADP
pH 8.0, 30°C, recombinant isozyme PPK2-2
7.24
ADP
mutant enzyme D117N, pH and temperature not specified in the publication
9.1
ADP
-
pH 8.0, 30°C, wild-type enzyme
41.9
ADP
pH 8.5, temperature not specified in the publication
41.9
ADP
-
50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
210
ADP
-
isoform PPK2, pH and temperature not specified in the publication
317
ADP
wild-type enzyme, pH and temperature not specified in the publication
332
ADP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
622
ADP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
943
ADP
-
isoform PPK1, pH and temperature not specified in the publication
950
ADP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
971
ADP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
994
ADP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
2.49
AMP
mutant N121D, pH not specified in the publication, temperature not specified in the publication
7.1
AMP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.05
ATP
pH 8.5, temperature not specified in the publication
0.05
ATP
-
50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
44.6
ATP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
45
ATP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
45.6
ATP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
46.9
ATP
-
isoform PPK1, pH and temperature not specified in the publication
55
ATP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
55.4
ATP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
74
ATP
-
pH 7.2, 30°C, recombinant wild-type enzyme
0.55
dADP
pH 8.0, 30°C
0.06
dAMP
pH 8.0, 30°C
0.0883
GDP
-
pH 7.2, 37°C
0.482
GDP
-
pH 7.5, 37°C, guanosine 5'-tetraphosphate synthesis
4.18
GDP
pH 8.0, 30°C, recombinant isozyme PPK2-1
645
GDP
-
isoform PPK1, pH and temperature not specified in the publication
0.8
GMP
pH 8.0, 30°C
0.08
GTP
-
50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
34
GTP
-
pH 7.2, 30°C, recombinant wild-type enzyme
1.04
Polyphosphate
-
pH 7.5, 37°C, guanosine 5'-tetraphosphate synthesis
77
Polyphosphate
-
pH 7.2, 30°C, recombinant wild-type enzyme
5.6
polyphosphate(4)
-
pH 8.0, 30°C, wild-type enzyme
-
15
polyphosphate(4)
pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T
-
0.31
polyphosphate25
-
pH 8.0, 37°C, truncated enzyme
4.28
polyphosphate25
-
pH 8.0, 37°C, full-length enzyme
0.29
polyphosphate65
-
pH 8.0, 37°C, truncated enzyme
-
3.93
polyphosphate65
-
pH 8.0, 37°C, full-length enzyme
-
0.117
UDP
-
pH 7.2, 37°C
4.9
UDP
pH 8.0, 30°C, recombinant isozyme PPK2-3
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8400
(phosphate)46
pH 8.5, temperature not specified in the publication
-
3.7 - 8400
(phosphate)65
-
8300
(phosphate)66
pH 8.5, temperature not specified in the publication
-
100 - 10200
(phosphate)n+1
0.37 - 0.79
polyphosphate(4)
-
92.3 - 1376.2
polyphosphate25
93.3 - 1578.3
polyphosphate65
-
1.37
UDP
pH 8.0, 30°C, recombinant isozyme PPK2-3
4
(phosphate)45
pH 8.5, temperature not specified in the publication
-
4
(phosphate)45
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
8300
(phosphate)45
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
3.7
(phosphate)65
pH 8.5, temperature not specified in the publication
-
3.704
(phosphate)65
-
polyphosphate synthesis reaction, in 50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
-
8400
(phosphate)65
-
polyphosphate utilization reaction, in 50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
-
100
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
500
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
10200
(phosphate)n+1
pH 8.0, 30°C, cosubstrate: ADP
0.00037
ADP
mutant enzyme R118A, pH and temperature not specified in the publication
0.00037
ADP
mutant R118A, pH not specified in the publication, temperature not specified in the publication
0.00044
ADP
mutant enzyme K66A, pH and temperature not specified in the publication
0.00044
ADP
mutant K66A, pH not specified in the publication, temperature not specified in the publication
0.00047
ADP
mutant D192A, pH not specified in the publication, temperature not specified in the publication
0.00047
ADP
mutant enzyme D192A, pH and temperature not specified in the publication
0.00095
ADP
mutant enzyme R178A, pH and temperature not specified in the publication
0.00095
ADP
mutant R178A, pH not specified in the publication, temperature not specified in the publication
0.0064
ADP
mutant D62A, pH not specified in the publication, temperature not specified in the publication
0.00643
ADP
mutant enzyme D62A, pH and temperature not specified in the publication
0.018
ADP
mutant D117N, pH not specified in the publication, temperature not specified in the publication
1.26
ADP
pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T
2.08
ADP
pH 8.0, 30°C, recombinant isozyme PPK2-2
4.1
ADP
mutant N121D, pH not specified in the publication, temperature not specified in the publication
5.79
ADP
wild-type, pH not specified in the publication, temperature not specified in the publication
5.79
ADP
wild-type enzyme, pH and temperature not specified in the publication
25.5
ADP
-
isoform PPK2, pH and temperature not specified in the publication
33.2
ADP
mutant enzyme D117N, pH and temperature not specified in the publication
33.2
ADP
mutant enzyme N121D, pH and temperature not specified in the publication
49
ADP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
100
ADP
wild-type, pH not specified in the publication, temperature not specified in the publication
110
ADP
pH 8.5, temperature not specified in the publication
110
ADP
-
50 mM Tris-HCl (pH 8.5), 30 mM MgCl2, at 25°C
214.2
ADP
wild-type enzyme, pH and temperature not specified in the publication
303.3
ADP
-
pH 8.0, 30°C, wild-type enzyme
998
ADP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
3529
ADP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
4690
ADP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
5222
ADP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
5743
ADP
-
isoform PPK1, pH and temperature not specified in the publication
4.106
AMP
mutant enzyme N121D, pH and temperature not specified in the publication
33.2
AMP
mutant N121D, pH not specified in the publication, temperature not specified in the publication
100
AMP
wild-type enzyme, pH and temperature not specified in the publication
214.2
AMP
wild-type, pH not specified in the publication, temperature not specified in the publication
0.1
ATP
pH 8.0, 30°C
0.15
ATP
pH 8.5, temperature not specified in the publication
0.15
ATP
-
50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
4.2
ATP
-
mutant Y524A of isoform PPK1, pH and temperature not specified in the publication
10.5
ATP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
29
ATP
-
mutant H510Q of isoform PPK1, pH and temperature not specified in the publication
31
ATP
-
mutant H480A of isoform PPK1, pH and temperature not specified in the publication
32.6
ATP
-
mutant H480Q of isoform PPK1, pH and temperature not specified in the publication
34.7
ATP
-
isoform PPK1, pH and temperature not specified in the publication
1.1
dADP
pH 8.0, 30°C
0.1
dAMP
pH 8.0, 30°C
0.1
GDP
pH 8.0, 30°C
3.48
GDP
pH 8.0, 30°C, recombinant isozyme PPK2-1
57
GDP
-
isoform PPK1, pH and temperature not specified in the publication
0.1
GMP
pH 8.0, 30°C
0.121
GTP
-
50 mM Tris-HCl (pH 8.5), 1 mM MnCl2, at 25°C
0.37
polyphosphate(4)
-
pH 8.0, 30°C, wild-type enzyme
-
0.79
polyphosphate(4)
pH 8.0, 30°C, mutant enzyme H102K/A106E/V115T
-
92.3
polyphosphate25
-
pH 8.0, 37°C, truncated enzyme
1376.2
polyphosphate25
-
pH 8.0, 37°C, full-length enzyme
93.3
polyphosphate65
-
pH 8.0, 37°C, truncated enzyme
-
1578.3
polyphosphate65
-
pH 8.0, 37°C, full-length enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.064 - 0.975
(2-anilinoethane-1,1-diyl)bis(phosphonic acid)
0.085 - 0.752
(2E)-2-[(4-nitrophenyl)methylidene]-4,4-diphosphonobutanoic acid
0.000039
G-quadruplex thrombin binding aptamer
Mycobacterium tuberculosis
pH 8.5, temperature not specified in the publication
-
0.262
[(2,3-dichloroanilino)methylene]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.216
[(3,5-dichloroanilino)methylene]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.071 - 0.103
[(3-aminoanilino)methylene]bis(phosphonic acid)
0.058 - 0.468
[(3-carbamimidamidoanilino)methylene]bis(phosphonic acid)
0.06
[(4-benzylanilino)methylene]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.645
[2-(2,3-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.058 - 0.269
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
0.147 - 0.935
[2-(3-chloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
0.107
[2-(3-nitroanilino)ethane-1,1-diyl]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.085 - 0.354
[2-[(1-amino-2-methylbutyl)(hydroxy)phosphoryl]ethyl]phosphonic acid
0.064
(2-anilinoethane-1,1-diyl)bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.975
(2-anilinoethane-1,1-diyl)bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.085
(2E)-2-[(4-nitrophenyl)methylidene]-4,4-diphosphonobutanoic acid
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.752
(2E)-2-[(4-nitrophenyl)methylidene]-4,4-diphosphonobutanoic acid
Escherichia coli
pH 8, temperature not specified in the publication
0.071
[(3-aminoanilino)methylene]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.103
[(3-aminoanilino)methylene]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.058
[(3-carbamimidamidoanilino)methylene]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.468
[(3-carbamimidamidoanilino)methylene]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.058
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.184
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.269
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.147
[2-(3-chloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
0.935
[2-(3-chloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.085
[2-[(1-amino-2-methylbutyl)(hydroxy)phosphoryl]ethyl]phosphonic acid
Escherichia coli
pH 8, temperature not specified in the publication
0.354
[2-[(1-amino-2-methylbutyl)(hydroxy)phosphoryl]ethyl]phosphonic acid
Cytophaga hutchinsonii
pH 8, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0
Thermosynechococcus vestitus
of the purified protein
0.00067
-
GTP formation from GDP, pH 7.0, 37°C, wild-type clone AG83
0.0012
-
GTP formation from GDP, pH 7.0, 37°C, SSG-resistant clone AG83
0.00208
-
GTP formation from GDP, pH 7.0, 37°C, PMM-resistant clone AG83
0.0055
polyphosphate kinase 2
0.0335
-
ATP formation from ADP, pH 7.0, 37°C, PMM-resistant clone AG83
0.034
recombinant polyphosphate kinase
0.0369
-
ATP formation from ADP, pH 7.0, 37°C, SSG-resistant clone AG83
0.0442
-
ATP formation from ADP, pH 7.0, 37°C, wild-type clone AG83
0.13
-
polyphosphate kinase activity in crude extracts measured with a modified toluidine blue assay
0.25
synthesis of ATP, pH 8, 37°C
0.317
Thermosynechococcus vestitus
purified recombinant His-tagged Ppk
0.7
-
synthesis of ATP, reversed reaction
1.8
substrate ADP, pH 7, 70°C
14
-
purified recombinant wild-type enzyme, polyphosphate synthesis with GTP
15
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 80 mM K+
18
-
purified recombinant wild-type enzyme, polyphosphate synthesis with ITP
20
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 80 mM K+
26.7
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 25 mM NH4+
31
-
purified recombinant wild-type enzyme, polyphosphate synthesis with ATP
3126.7
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 80 mM K+
3150
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 25 mM NH4+
32
-
purified recombinant wild-type enzyme, polyphosphate dephosphorylation
3223.3
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+
35
-
recombinant full-length enzyme, pH 8.0, 37°C, ATP formation, in presence of 25 mM NH4+
4.2
-
of the recombinant protein
474
synthesis of polyphosphate, pH 7.2, 37°C
645
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 80 mM K+
655
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+
715
-
recombinant truncated enzyme, pH 8.0, 37°C, ATP formation, in presence of 5 mM Mg2+ and 25 mM NH4+
99.1
substrate AMP, pH 7, 70°C
0.15
-
-
189
pH 7.0, 30°C
189
synthesis of ATP, pH 7, 30°C
189
synthesis of ATP, pH 7, 30°C
additional information
-
-
additional information
-
relative activity of mutant enzymes compared to the wild-type in both reaction directions, overview
additional information
-
-
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-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
Oryza sativa Japonica Group cv. Wuyugeng 7
-
-
-
brenda
additional information
wild-type enzyme activity increases significantly as the bacteria transition from log to stationary phase
brenda
additional information
-
wild-type enzyme activity increases significantly as the bacteria transition from log to stationary phase
brenda
additional information
-
wild-type enzyme activity increases significantly as the bacteria transition from log to stationary phase
-
brenda
additional information
-
planktonic cells and cells in a biofilm
brenda
additional information
-
planktonic cells and cells in a biofilm
-
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
additional information
the relative distributions of Candidatus Accumulibacter clades vary among different enhanced biological phosphorus removal systems and also temporally within a system
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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drug target
bacterial species, including many pathogens, encode a homolog of a major polyP synthesis enzyme, polyphosphate kinase (PPK) with 2 different genes coding for PPK1 and PPK2. Genetic deletion of the ppk1 gene leads to reduced polyP levels and the consequent loss of virulence and stress adaptation responses. No PPK1 homolog has been identified in higher-order eukaryotes, and, therefore, PPK1 represents a target for chemotherapy
drug target
polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
drug target
polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
-
drug target
-
polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
-
drug target
-
polyphosphate kinases are involved in many metabolic processes in bacteria, including pathogenic species. As these enzymes are not present in animals, they are a prime target for the development of antibiotics
-
drug target
-
bacterial species, including many pathogens, encode a homolog of a major polyP synthesis enzyme, polyphosphate kinase (PPK) with 2 different genes coding for PPK1 and PPK2. Genetic deletion of the ppk1 gene leads to reduced polyP levels and the consequent loss of virulence and stress adaptation responses. No PPK1 homolog has been identified in higher-order eukaryotes, and, therefore, PPK1 represents a target for chemotherapy
-
evolution
a polyphosphate kinase from the polyphosphate kinase 2 (PPK2) family. The enzyme structure consists of a six-stranded parallelbeta-sheet surrounded by 12 alpha-helices, with a high degree of similarity to other members of the PPK2 family and the thymidylate kinase superfamily
evolution
in general, all PPKs are ancient enzymes, and phylogenetic analysis indicates that the polyphosphate degradation process is older than polyphosphate synthesis. Additionally, PPK2 proteins are older than PPK1 enzymes
evolution
-
in general, all PPKs are ancient enzymes, and phylogenetic analysis indicates that the polyphosphate degradation process is older than polyphosphate synthesis. Additionally, PPK2 proteins are older than PPK1 enzymes
-
malfunction
-
a mutant lacking ppk is more than 10fold less competitive against wild type Pf0-1 in sterile loam soil low in inorganic phosphate, while a ppk and nonpredicted antisense RNA mutant of Pf0-1 does not have increased sensitivity to osmotic, oxidative, and acid stress, it is more sensitive to elevated temperatures in laboratory medium and during growth in sterile soil
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
-
deletion of ppk1 causes loss of virulence for animals
malfunction
deletion of ppk1 causes loss of virulence for animals
malfunction
-
mutants lacking PPK1 are defective in motility, quorum sensing, biofilm formation, and virulence
malfunction
-
PPK1 knockout mutant cells lacking polyphosphate survive poorly during growth in the stationary phase and are less resistant to heat, oxidants, osmotic challenge, antibiotics and UV
malfunction
-
ppk1-knockout mutant is deficient in poly-P accumulation, which is associated with a decreased ability to form viable-but-nonculturable cells under acid stress. The ppk1-deficient mutant shows a significant increase in susceptibility to erythromycin, cefotaxime, ciprofloxacin, rifampin, polymyxin B, tetracycline, cholic acid, taurocholic acid, deoxycholic acid, ethidium bromide, and SDS
malfunction
-
the isogenic in-frame ppk1 deletion mutant PD44 shows poor survival rates during osmotic shock and acidic challenge and is defective in bacterial adhesion and translocation across the blood-brain-barrier
malfunction
-
the polyphosphate kinase mutant is susceptible to hydrogen peroxide in an oxidative stress condition, unable to perform swimming, swarming motilities, and has lower density biofilm forming capacity than the wild type strain
malfunction
-
under phosphate limitation conditions, the double polyphosphate kinase/phosphate-binding protein mutant shows a higher production of the endogenous antibiotic actinorhodin and the heterologous antitumor 8-demethyl-tetracenomycin (up to 10fold with respect to the wild type strain)
malfunction
deletion of gene ppk results in a deficiencyin polyphosphate accumulation rather than cell growth in Luria-Bertani medium. The cell growth is evidently retarded and the ilvBHC expression is significantly reduced when the ppk mutant is transferred from LB to limited-amino acid medium. These phenotypes are significantly restored in the ppk-complemented strain
malfunction
-
planktonic cells of a ppk knockout strain (DELTAppk) are more susceptible to antibiotics than the wild-type strain, while biofilm-grown DELTAppk cells show similar susceptibility compared to the wild-type and are more tolerant than the planktonic cells. Phenotypes, overview
malfunction
Q9S646
Pseudomonas aeruginosa strains wild-type MPAO1 and enzyme-deficient PW9825 survival in oxidative stress, overview
malfunction
the isogenic deletion mutant is defective for intracellular growth in macrophages and is attenuated in mice. The DELTAFTT1564 strain shows significantly increased sensitivity to a range of antibiotics in a manner independent of the mode of action of the antibiotic
malfunction
the ppk-deficient mutant is deficient in resistance to oxidative, hyperosmotic and heat stress. The swarming and biofilm formation abilities of Proteus mirabilis are also attenuated after the ppk interruption. Negative phenotypes of the ppk mutant can be restored by ppk gene complementation
malfunction
a mutant lacking the enzyme (PPK) makes no detectable polyP under any condition
malfunction
gene deletion alters specific metabolic pathways, changing the metabolic fingerprint, and suppressing the ability of Escherichia coli to form a biofilm
malfunction
-
mutation of ES2/OsIPK2 gene results to increased H2O2 and malondialdehyde content and catalase (CAT), superoxide dismutase (SOD), peroxidase (POD) and ascorbate peroxidase (APX) activity, and to reduced chlorophyll and Net photosynthetic rate, which eventually leads to leaf senescence and reduced rice yield
malfunction
-
polyphosphate kinase deletion causes decreased resistance to oxidative, heat and hyperosmotic stress, attenuated swarming and biofilm formation, increased production of prolyl isomerase, phosphotransferase and peptidoglycan synthase repressor proteins
malfunction
-
polyphosphate kinase deletion causes decreased virulence and low invasiveness
malfunction
-
polyphosphate kinase deletion causes loss of biofilm formation on polyvinyl chloride (PVC) or borosilicate
malfunction
-
polyphosphate kinase deletion decreases sporulation, motility and biofilm formation
malfunction
-
polyphosphate kinase deletion increases sensitivity to H2O2 and reduces polyphosphate accumulation. Polyphosphate kinase deletion upregulates fermentation, aerobic and anaerobic respiration, enhances catalase and Clp protease activity, down-regulates ATP-dependent RNA helicase, DNA polymerase III and pyruvate kinase I
malfunction
-
polyphosphate kinase ppk1 deletion causes loss of virulence and biofilm formation, impaired motility and increased susceptibility to antibiotics. Polyphosphate kinase ppk2 deletion causes increased susceptibility to antibiotics
malfunction
-
polyphosphate kinase ppk1 deletion causes low polyphosphate accumulation, loss of virulence, reduced colonization in mice and decreased motility
malfunction
-
polyphosphate kinase ppk1 deletion causes poor survival during osmotic shock and acid challenge
malfunction
-
polyphosphate kinase ppk1 deletion increases serum sensitivity
malfunction
-
polyphosphate kinase ppk2 deletion causes increased sensitivity to antibiotics
malfunction
ppk-2 mutant strain infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild type infected guinea pigs at later stages of infection. The ppk-2 mutant strainis more tolerant to isoniazid and impaired for survival in THP-1 macrophages
malfunction
-
the isogenic in-frame ppk1 deletion mutant PD44 shows poor survival rates during osmotic shock and acidic challenge and is defective in bacterial adhesion and translocation across the blood-brain-barrier
-
malfunction
-
polyphosphate kinase deletion increases sensitivity to H2O2 and reduces polyphosphate accumulation. Polyphosphate kinase deletion upregulates fermentation, aerobic and anaerobic respiration, enhances catalase and Clp protease activity, down-regulates ATP-dependent RNA helicase, DNA polymerase III and pyruvate kinase I
-
malfunction
-
polyphosphate kinase ppk1 deletion causes poor survival during osmotic shock and acid challenge
-
malfunction
-
the ppk-deficient mutant is deficient in resistance to oxidative, hyperosmotic and heat stress. The swarming and biofilm formation abilities of Proteus mirabilis are also attenuated after the ppk interruption. Negative phenotypes of the ppk mutant can be restored by ppk gene complementation
-
malfunction
-
under phosphate limitation conditions, the double polyphosphate kinase/phosphate-binding protein mutant shows a higher production of the endogenous antibiotic actinorhodin and the heterologous antitumor 8-demethyl-tetracenomycin (up to 10fold with respect to the wild type strain)
-
malfunction
-
a mutant lacking ppk is more than 10fold less competitive against wild type Pf0-1 in sterile loam soil low in inorganic phosphate, while a ppk and nonpredicted antisense RNA mutant of Pf0-1 does not have increased sensitivity to osmotic, oxidative, and acid stress, it is more sensitive to elevated temperatures in laboratory medium and during growth in sterile soil
-
malfunction
-
ppk-2 mutant strain infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild type infected guinea pigs at later stages of infection. The ppk-2 mutant strainis more tolerant to isoniazid and impaired for survival in THP-1 macrophages
-
malfunction
-
ppk-2 mutant strain infected guinea pigs have significantly reduced bacterial loads and tissue pathology in comparison to wild type infected guinea pigs at later stages of infection. The ppk-2 mutant strainis more tolerant to isoniazid and impaired for survival in THP-1 macrophages
-
malfunction
Oryza sativa Japonica Group cv. Wuyugeng 7
-
mutation of ES2/OsIPK2 gene results to increased H2O2 and malondialdehyde content and catalase (CAT), superoxide dismutase (SOD), peroxidase (POD) and ascorbate peroxidase (APX) activity, and to reduced chlorophyll and Net photosynthetic rate, which eventually leads to leaf senescence and reduced rice yield
-
malfunction
-
planktonic cells of a ppk knockout strain (DELTAppk) are more susceptible to antibiotics than the wild-type strain, while biofilm-grown DELTAppk cells show similar susceptibility compared to the wild-type and are more tolerant than the planktonic cells. Phenotypes, overview
-
malfunction
-
ppk1-knockout mutant is deficient in poly-P accumulation, which is associated with a decreased ability to form viable-but-nonculturable cells under acid stress. The ppk1-deficient mutant shows a significant increase in susceptibility to erythromycin, cefotaxime, ciprofloxacin, rifampin, polymyxin B, tetracycline, cholic acid, taurocholic acid, deoxycholic acid, ethidium bromide, and SDS
-
malfunction
-
a mutant lacking the enzyme (PPK) makes no detectable polyP under any condition
-
malfunction
-
gene deletion alters specific metabolic pathways, changing the metabolic fingerprint, and suppressing the ability of Escherichia coli to form a biofilm
-
malfunction
-
the polyphosphate kinase mutant is susceptible to hydrogen peroxide in an oxidative stress condition, unable to perform swimming, swarming motilities, and has lower density biofilm forming capacity than the wild type strain
-
metabolism
-
cell growth, hydrogen productivity and cellular metabolism of Enterobacter aerogenes IAM1183 are affected by the external addition of diphosphate and the overexpression of the enzyme at different initial glucose concentrations
metabolism
identification of a protein PhaX as a putative link between poly(3-hydroxybutyrate) and polyphospate metabolism, the A2274 (phaX) gene product is annotated as a hypothetical putative phosphate transport regulator, regulation, overview. Polyphosphate granules in Ralstonia eutropha are often located in the neighborhood of polyhydroxybutyrate granules if both biopolymers are present simultaneously
metabolism
PPK is a primary enzyme involved in polyphosphate biosynthesis
metabolism
-
identification of a protein PhaX as a putative link between poly(3-hydroxybutyrate) and polyphospate metabolism, the A2274 (phaX) gene product is annotated as a hypothetical putative phosphate transport regulator, regulation, overview. Polyphosphate granules in Ralstonia eutropha are often located in the neighborhood of polyhydroxybutyrate granules if both biopolymers are present simultaneously
-
physiological function
-
polyphosphate kinase is necessary for optimal competitive fitness in LB broth culture and sterile loam soil
physiological function
PPK1 regulates error-prone DNA replication by DNA polymerase IV, leading to adaptive mutation
physiological function
-
polyphosphate kinase 1 is required for the pathogenesis process of meningitic Escherichia coli K1 (RS218) and plays an important role in stress adaption and virulence
physiological function
-
polyphosphate kinase plays a role in virulence, such as in oxidative stress response, motilities and biofilm formation. Polyphosphate kinase is also essential and independently involved in biofilm formation
physiological function
enzyme PPK is an important regulator and plays a crucial role in stress tolerance and virulence in uropathogenic Proteus mirabilis, overview. Gene ppk is required for Proteus mirabilis to invade the bladder
physiological function
-
enzyme PPK is important for the antibiotic stress response during the planktonic growth of extraintestinal pathogenic Escherichia coli
physiological function
important role for polyphosphate in the virulence of Francisella
physiological function
polyphosphate is essential for cell growth and responses to nutritional stringen-cies and environmental stresses and branched-chain amino acids are useful intracellular signals for bacterial adaption to nutritional environments. Enzyme PPK plays a rolein polyphosphate accumulation and expression of genes involved in branched-chain amino acids biosynthesis
physiological function
polyphosphate kinase 1 is a central node in the stress response network of Mycobacterium tuberculosis, it connects the two-component systems MprAB and SenX3-RegX3 and the extracytoplasmic function sigma factor, sigma E, overview. Role of SigE in ppk1 transcription, while enzyme PPK1 is itself capable of regulating sigE expression via the MprAB TCS, presence of multiple positive feedback loops in this signalling circuit. Gene ppk1 is induced during phosphate limitation in Mycobacterium tuberculosis
physiological function
Q9S646
polyphosphate kinase 1 plays an important role in virulence, antibiotic resistance and survival under stress conditions
physiological function
-
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
physiological function
a PPK2 mutant strain shows significantly increased sensitivity to a range of antibiotics in a manner independent of the mode of action of the antibiotic
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
physiological function
-
in Escherichia coli polyphosphate levels are controlled via the polyphosphate-synthesizing enzyme polyphosphate kinase (PPK1) and exopolyphosphatases (PPX and GPPA), and are temporarily enhanced by PPK1 overexpression and reduced by PPX overexpression
physiological function
polyphosphate kinase is a negative regulator of virulence gene expression in Francisella tularensis
physiological function
-
polyphosphate kinases catalyzes the polyphosphate formation or ATP formation, to store energy or to regenerate ATP, respectively
physiological function
polyphosphate kinases catalyzes the polyphosphate formation or ATP formation, to store energy or to regenerate ATP, respectively
physiological function
PPK-2 enzyme is required for Mycobacterium tuberculosis growth during acute and chronic stage of infection. PPK-2 enzyme contributes to the ability of Mycobacterium tuberculosis to cause disease in guinea pigs
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
physiological function
-
the ES2 gene, encoding an inositol polyphosphate kinase localized in the nucleus and plasma membrane of cells, is essential for leaf senescence in rice
physiological function
-
polyphosphate kinase is a negative regulator of virulence gene expression in Francisella tularensis
-
physiological function
-
polyphosphate kinase 1 is required for the pathogenesis process of meningitic Escherichia coli K1 (RS218) and plays an important role in stress adaption and virulence
-
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
-
physiological function
-
enzyme PPK is an important regulator and plays a crucial role in stress tolerance and virulence in uropathogenic Proteus mirabilis, overview. Gene ppk is required for Proteus mirabilis to invade the bladder
-
physiological function
-
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
-
physiological function
-
polyphosphate kinase is necessary for optimal competitive fitness in LB broth culture and sterile loam soil
-
physiological function
-
polyphosphate kinase 1 is a central node in the stress response network of Mycobacterium tuberculosis, it connects the two-component systems MprAB and SenX3-RegX3 and the extracytoplasmic function sigma factor, sigma E, overview. Role of SigE in ppk1 transcription, while enzyme PPK1 is itself capable of regulating sigE expression via the MprAB TCS, presence of multiple positive feedback loops in this signalling circuit. Gene ppk1 is induced during phosphate limitation in Mycobacterium tuberculosis
-
physiological function
-
PPK-2 enzyme is required for Mycobacterium tuberculosis growth during acute and chronic stage of infection. PPK-2 enzyme contributes to the ability of Mycobacterium tuberculosis to cause disease in guinea pigs
-
physiological function
-
PPK-2 enzyme is required for Mycobacterium tuberculosis growth during acute and chronic stage of infection. PPK-2 enzyme contributes to the ability of Mycobacterium tuberculosis to cause disease in guinea pigs
-
physiological function
Oryza sativa Japonica Group cv. Wuyugeng 7
-
the ES2 gene, encoding an inositol polyphosphate kinase localized in the nucleus and plasma membrane of cells, is essential for leaf senescence in rice
-
physiological function
-
enzyme PPK is important for the antibiotic stress response during the planktonic growth of extraintestinal pathogenic Escherichia coli
-
physiological function
-
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
-
physiological function
-
polyphosphate kinase plays a role in virulence, such as in oxidative stress response, motilities and biofilm formation. Polyphosphate kinase is also essential and independently involved in biofilm formation
-
physiological function
Francisella tularensis Schu 4
-
besides adenosine 5'-triphosphate, PPK2s also catalyses the synthesis of highly phosphorylated nucleotides in vitro, such as adenosine 5'-tetraphosphate and adenosine 5'-pentaphosphate
-
additional information
a lid-loop and the conserved Walker A and B motifs are important for substrate binding and enzyme catalysis
additional information
-
homology structural model of full-length paPpx, in closed conformation, and of the N-terminal domain of paPpx in an open state, constructed by comparative modeling, molecular dynamic simulations, overview. Docking study with bound metals and/or ADP defining the N-paPpx(1-314) model in open conformation as receptor, docking with polyphosphate and ADP. Enzyme electrostatic potential calculations. A model of the paPpx N-terminal domain in complex with a polyP chain of 7 residues long and a molecule of ADP explains the phosphotransferase activity through docking techniques, overview
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hexamer
6 * 118000, SDS-PAGE, DdPPK1 forms higher oligomeric structures in the presence of either poly phosphate or ATP
?
x * 36200, about, sequence calculation
?
x * 30700, about, sequence calculation
?
x * 31100, about, sequence calculation
?
x * 33900, about, sequence calculation
?
x * 42100, about, sequence calculation
?
x * 78200, about, sequence calculation
?
x * 79600, about, sequence calculation
?
-
x * 79600, about, sequence calculation
-
?
-
x * 78200, about, sequence calculation
-
?
-
x * 30700, about, sequence calculation
-
?
-
x * 33900, about, sequence calculation
-
?
-
x * 42100, about, sequence calculation
-
?
-
x * 36200, about, sequence calculation
-
?
-
x * 31100, about, sequence calculation
-
?
x * 44000, SDS-PAGE, recombinant protein
?
-
x * 44000, SDS-PAGE, recombinant protein
-
?
x * 32000, SDS-PAGE, x * 31600, calculated from sequence
?
-
x * 32000, SDS-PAGE, x * 31600, calculated from sequence
-
?
x * 41000, SDS-PAGE, recombinant protein
?
-
x * 41000, SDS-PAGE, recombinant protein
-
?
x * 40800, deduced from nucleotide sequence
?
x * 60000, denatured His-tagged protein
?
-
x * 56419, sequence calculation, wild-type, full-length enzyme
?
x * 40800, calculated from sequence
?
-
x * 60000, denatured His-tagged protein
-
?
-
x * 40800, calculated from sequence
-
?
x * 70000, calculation from nucleotide sequence
?
-
x * 57000, glycogen-complexed enzyme, SDS-PAGE
dimer
-
-
homodimer
-
2 * 87000, isoform PPK1, SDS-PAGE
homodimer
-
x-ray crystallography
homotetramer
-
4 x 39000, SDS PAGE
homotetramer
-
4 x 39000, SDS PAGE
-
homotetramer
-
4 * 81000, gel filtration
homotetramer
x-ray crystallography
monomer
-
1 * 79000, SDS-PAGE
monomer
behaves as a monomer in the absence of substrate, but addition of polyphosphate promotes dimerization
monomer
-
behaves as a monomer in the absence of substrate, but addition of polyphosphate promotes dimerization
-
monomer
-
1 * 85000, SDS-PAGE
monomer
1 * 34750, recombinant PPK2-3, sequence calculation and SDS-PAGE
monomer
1 * 36720, recombinant PPK2-1, sequence calculation and SDS-PAGE
monomer
1 * 39950, recombinant PPK2-2, sequence calculation and SDS-PAGE
monomer
-
1 * 36720, recombinant PPK2-1, sequence calculation and SDS-PAGE
-
monomer
-
1 * 39950, recombinant PPK2-2, sequence calculation and SDS-PAGE
-
monomer
-
1 * 34750, recombinant PPK2-3, sequence calculation and SDS-PAGE
-
octamer
-
gel filtration
octamer
-
gel filtration
-
octamer
-
8 * 41000, in presence of P15, octamer is unstable
octamer
-
8 * 41000, in presence of P15, octamer is unstable
-
tetramer
-
PPK2B is active as a homotetramer
tetramer
-
PPK2B is active as a homotetramer
-
tetramer
-
4 * 69000, SDS-PAGE
tetramer
tetrameric in the crystalline state
tetramer
-
tetrameric in the crystalline state
-
tetramer
tetrameric in the crystalline state. Trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
tetramer
-
tetrameric in the crystalline state. Trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
-
tetramer
4 * 44000, SDS-PAGE, 4 * 40786, calculated from sequence
tetramer
-
4 * 44000, SDS-PAGE, 4 * 40786, calculated from sequence
-
trimer
trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
trimer
-
trimeric in solution the absence of substrates, but forms tetramers in the presence of polyphosphate
-
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
proteome analysis of PPK motif proteins, overview
additional information
-
proteome analysis of PPK motif proteins, overview
-
additional information
the enzyme from Dictyostelium discoideum has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
additional information
-
the enzyme from Dictyostelium discoideum has an unique N-terminal extension of 370 amino acids, lacking homology with any known protein, that is necessary for its enzymatic activity, cellular localization, and physiological functions, overview
additional information
the structure consists of a six-stranded parallel beta-sheet surrounded by 12 alpha-helices, with a high degree of similarity to other members of the PPK2 family and the thymidylate kinase superfamily
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D230N
the variant has somewhat greater processivity than the wild-type enzyme
E173K
the variant has somewhat greater processivity than the wild-type enzyme
E245K
mutation leads to very high polyP accumulation in vivo but is not different from the wild type in either activity or chain length of polyP produced in vitro
F488A
-
complete loss of all 4 polyphosphate kinase activities
P507A
-
complete loss of all 4 polyphosphate kinase activities
Q674A
-
complete loss of all 4 polyphosphate kinase activities
R375A
-
complete loss of all 4 polyphosphate kinase activities
R564A
-
complete loss of all 4 polyphosphate kinase activities
R621A
-
complete loss of all 4 polyphosphate kinase activities
S380A
-
complete loss of all 4 polyphosphate kinase activities
Y468A
-
120-140% of wild-type polyphosphate, GTP, and guanosine 5'-tetraphosphate synthesis activity, 20-50% of wild-type ATP synthesis activity
D230N
-
the variant has somewhat greater processivity than the wild-type enzyme
-
E173K
-
the variant has somewhat greater processivity than the wild-type enzyme
-
E245K
-
mutation leads to very high polyP accumulation in vivo but is not different from the wild type in either activity or chain length of polyP produced in vitro
-
D62A
-
about 1000fold decrease in activity
-
E126G
about 18% of wild-type activity with substrate AMP, about 40% of wild-type activity with ADP
E126N
about 5% of wild-type activity with substrate AMP, bout 15% of wild-type activity with ADP
E126G
-
about 18% of wild-type activity with substrate AMP, about 40% of wild-type activity with ADP
-
E126N
-
about 5% of wild-type activity with substrate AMP, bout 15% of wild-type activity with ADP
-
N121D
-
7fold decrease in activity with AMP, 25fold decrease in activity with ADP
-
A615S
-
the mutant exhibits about wild type activity for ATP synthesis and polyphosphate synthesis
E681A
-
the mutant exhibits less than 5% activity for ATP synthesis and less than 30% activity for polyphosphate synthesis compared o the wild type enzyme
F125A
the proteins has significantly reduced activity as compared to wild type protein
F67A
-
84% activity compared to the wild type enzyme
G69R
-
67.1% activity compared to the wild type enzyme
G72A
the activity of MBP-G72APPK-2 and wild type proteins are similar
G74R
-
7.6% activity compared to the wild type enzyme, the mutant enzyme cannot interact with nucleoside diphosphate kinase
H115A
-
49% activity compared to the wild type enzyme
H115A/H247A
-
6% activity compared to the wild type enzyme
H150A
-
the mutation causes PPK1 protein deficient but not defective in autophosphorylation and severely affects ATP or polyphosphate synthesis
H150Q
-
the mutation causes PPK1 protein deficient but not defective in autophosphorylation and mildly affects ATP or polyphosphate synthesis
H247A
-
38% activity compared to the wild type enzyme
H480A
-
the mutant catalytic efficiency for the polyphosphate synthesis is almost or very close to that of the wild type enzyme
H480Q
-
the mutant catalytic efficiency for the polyphosphate synthesis is almost or very close to that of the wild type enzyme
H510Q
-
the mutant catalytic efficiency for the polyphosphate synthesis is almost or very close to that of the wild type enzyme
K75A
-
89% activity compared to the wild type enzyme
N515A
-
the mutant exhibits less than 2% activity for ATP synthesis and about 65% activity for polyphosphate synthesis compared to the wild type enzyme
R431A
-
the mutant exhibits less than 5% activity for ATP synthesis and about 78% activity for polyphosphate synthesis compared to the wild type enzyme
R461A
-
the mutant exhibits less than 2% activity for ATP synthesis and about 76% activity for polyphosphate synthesis compared to the wild type enzyme
R624A
-
the mutant exhibits less than 2% activity for ATP synthesis and about 65% activity for polyphosphate synthesis compared to the wild type enzyme
R654A
-
the mutant exhibits less than 1% activity for ATP synthesis and about 90% activity for polyphosphate synthesis compared to the wild type enzyme
S668A
-
the mutant exhibits less than 5% activity for ATP synthesis and less than 30% activity for polyphosphate synthesis compared to the wild type enzyme
W129A
the proteins has significantly reduced activity as compared to wild type protein
Y524A
-
the mutant exhibits less than 10% activity for ATP synthesis and less than 20% activity for polyphosphate synthesis compared to the wild type enzyme
F125A
-
the proteins has significantly reduced activity as compared to wild type protein
-
G72A
-
the activity of MBP-G72APPK-2 and wild type proteins are similar
-
W129A
-
the proteins has significantly reduced activity as compared to wild type protein
-
F125A
-
the proteins has significantly reduced activity as compared to wild type protein
-
F67A
-
84% activity compared to the wild type enzyme
-
G69R
-
67.1% activity compared to the wild type enzyme
-
G72A
-
the activity of MBP-G72APPK-2 and wild type proteins are similar
-
H115A
-
49% activity compared to the wild type enzyme
-
H247A
-
38% activity compared to the wild type enzyme
-
K75A
-
89% activity compared to the wild type enzyme
-
W129A
-
the proteins has significantly reduced activity as compared to wild type protein
-
D395A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
F176A
-
site-directed mutagenesis, highly reduced forward and reverse reaction activities compared to the wild-type enzyme
F176Y
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
G347A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
H491A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
H491A/H510A
-
site-directed mutagenesis, highly reduced forward and reverse reaction activities compared to the wild-type enzyme
H510A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
L234A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
P225A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
R230A
-
site-directed mutagenesis, highly reduced forward and reverse reaction activities compared to the wild-type enzyme
R230K
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
R309A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
G347A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
H510A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
-
R230K
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
G347A
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
H510A
-
site-directed mutagenesis, reduced forward and reverse reaction activities compared to the wild-type enzyme
-
R230K
-
site-directed mutagenesis, slightly reduced forward and reverse reaction activities compared to the wild-type enzyme
-
D307A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D320A
-
the mutant shows reduced activity compared to the wild type enzyme
D323A
-
the mutant shows reduced activity compared to the wild type enzyme
D362A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
D437A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
E304A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K311A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
K473A
-
the mutant shows reduced activity compared to the wild type enzyme
Q416A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R316A
-
the mutant shows reduced activity compared to the wild type enzyme
R325A
-
the mutant shows reduced activity compared to the wild type enzyme
R363A
-
the mutant shows almost no activity compared to the wild type enzyme
R419A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R423A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
R477A
-
the mutant shows increased activity compared to the wild type enzyme
W408A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
Y447A
-
the mutant shows strongly reduced activity compared to the wild type enzyme
A106E
mutant enzyme does not show any detectable activity
A106E/H102K
mutant enzyme does not show any detectable activity
A106E/V115T
mutant enzyme does not show any detectable activity
D148A
the mutant shows strongly reduced activity compared to the wild type enzyme
D223A
the mutant shows strongly reduced activity compared to the wild type enzyme
D93A
the mutant shows strongly reduced activity compared to the wild type enzyme
E90A
the mutant shows strongly reduced activity compared to the wild type enzyme
H102K
mutant enzyme does not show any detectable activity
H102K/A106E/V115T
mutant enzyme H102K/A106E/V115T exhibits the capability to utilize polyP(4) as phosphate donor to synthesize ATP. The wild-type enzyme can not adopt polyphosphate(4)
K97A
the mutant shows strongly reduced activity compared to the wild type enzyme
Q202A
the mutant shows strongly reduced activity compared to the wild type enzyme
R149A
the mutant shows strongly reduced activity compared to the wild type enzyme
R205A
the mutant shows strongly reduced activity compared to the wild type enzyme
R209A
the mutant shows strongly reduced activity compared to the wild type enzyme
R263A
the mutant shows almost wild type activity
V115T
mutant enzyme does not show any detectable activity
V115T/H102K
mutant enzyme does not show any detectable activity
W194A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y233A
the mutant shows strongly reduced activity compared to the wild type enzyme
D117N
about 300fold decrease in activity
D117N
catalytic efficiency (kcat/Km) is 5.7fold higher than wild-type value
D192A
about 10000fold decrease in activity
D192A
catalytic efficiency (kcat/Km) is 12319fold lower than wild-type value
D62A
about 1000fold decrease in activity
D62A
catalytic efficiency (kcat/Km) is 900fold lower than wild-type value
K66A
about 10000fold decrease in activity
K66A
catalytic efficiency (kcat/Km) is 131590fold lower than wild-type value
R118A
about 10000fold decrease in activity
R118A
catalytic efficiency (kcat/Km) is 15649fold lower than wild-type value
R178A
about 10000fold decrease in activity
R178A
catalytic efficiency (kcat/Km) is 6095fold lower than wild-type value
D192A
-
about 10000fold decrease in activity
-
D192A
-
catalytic efficiency (kcat/Km) is 12319fold lower than wild-type value
-
K66A
-
about 10000fold decrease in activity
-
K66A
-
catalytic efficiency (kcat/Km) is 131590fold lower than wild-type value
-
N121D
7fold decrease in activity with AMP, 25fold decrease in activity with ADP
N121D
the catalytic efficiency for ADP is 6.45fold lower than the wild-type value. The catalytic efficiency for AMP is 24fold lower than the wild-type value
N121D
-
7fold decrease in activity with AMP, 25fold decrease in activity with ADP
-
N121D
-
the catalytic efficiency for ADP is 6.45fold lower than the wild-type value. The catalytic efficiency for AMP is 24fold lower than the wild-type value
-
additional information
50% of the wild type gene are deleted, mutants reveal lower level of phosphorylated products and higher suceptibility to environmental stress
additional information
-
50% of the wild type gene are deleted, mutants reveal lower level of phosphorylated products and higher suceptibility to environmental stress
additional information
generation of a targeted ppk1 deletion mutant in Campylobacter jejuni strain 81-176, which exhibits low levels of polyphosphate at all growth stages in contrast to the wild-type enzyme. The DELTAppk1 mutant is defective for survival during osmotic shock and low-nutrient stress, phenotype, overview
additional information
-
generation of a targeted ppk1 deletion mutant in Campylobacter jejuni strain 81-176, which exhibits low levels of polyphosphate at all growth stages in contrast to the wild-type enzyme. The DELTAppk1 mutant is defective for survival during osmotic shock and low-nutrient stress, phenotype, overview
additional information
-
50% of the wild type gene are deleted, mutants reveal lower level of phosphorylated products and higher suceptibility to environmental stress
-
additional information
-
generation of a targeted ppk1 deletion mutant in Campylobacter jejuni strain 81-176, which exhibits low levels of polyphosphate at all growth stages in contrast to the wild-type enzyme. The DELTAppk1 mutant is defective for survival during osmotic shock and low-nutrient stress, phenotype, overview
-
additional information
-
ppk2A and ppk2b knockout organisms, ppk2b has PPK activity
additional information
-
deletion of ppk2B decreases PPK activity and cellular polyphosphate content, while overexpression of ppk2B increases both PPK activity and cellular polyphosphate content. Neither deletion nor overexpression of ppk2A changes specific activity of PPK or cellular polyphosphate content significantly. The ppk2B deletion mutant, which accumulated very little polyphopshate and grows like the wild-type under phosphate-sufficient conditions, shows a growth defect under phosphate-limiting conditions, phenotype, overview
additional information
-
ppk2A and ppk2b knockout organisms, ppk2b has PPK activity
-
additional information
-
deletion of ppk2B decreases PPK activity and cellular polyphosphate content, while overexpression of ppk2B increases both PPK activity and cellular polyphosphate content. Neither deletion nor overexpression of ppk2A changes specific activity of PPK or cellular polyphosphate content significantly. The ppk2B deletion mutant, which accumulated very little polyphopshate and grows like the wild-type under phosphate-sufficient conditions, shows a growth defect under phosphate-limiting conditions, phenotype, overview
-
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
additional information
-
construction of a chromosomal deletion strain of the enzyme, formation of polyphosphate and poly(3-hydroxybutyrate) granules in Ralstonia eutropha mutants during growth on NB-gluconate medium, overview
-
additional information
DdPPK1 mutants show reduced polyphosphate levels and are defective in fruiting body development, sporulation, and predation, and in late stages of cytokinesis and cell division, overview. The enzyme-defective mutants do not produce polyphosphate exopolymer
additional information
-
DdPPK1 mutants show reduced polyphosphate levels and are defective in fruiting body development, sporulation, and predation, and in late stages of cytokinesis and cell division, overview. The enzyme-defective mutants do not produce polyphosphate exopolymer
additional information
-
generation of a ppk knockout mutant strain, DELTAppk
additional information
-
generation of a ppk knockout mutant strain, DELTAppk
-
additional information
construction of a DELTA FTT1564 enzyme gene deletion mutant strain
additional information
construction of a ppk null mutant and the ppk-complemented strain, DELTAppk and DELTAppk (pHT304-ppk)
additional information
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construction of a ppk null mutant and the ppk-complemented strain, DELTAppk and DELTAppk (pHT304-ppk)
additional information
downregulation of ppk1 leads to impaired survival of Mycobacterium tuberculosis in macrophages, the stringent response regulator ppGpp is impaired in the ppk1 knockout mutant and is restored after complementation with ppk1 of Mycobacterium tuberculosis, overview
additional information
-
downregulation of ppk1 leads to impaired survival of Mycobacterium tuberculosis in macrophages, the stringent response regulator ppGpp is impaired in the ppk1 knockout mutant and is restored after complementation with ppk1 of Mycobacterium tuberculosis, overview
additional information
the ppk1 promoter of Mycobacterium tuberculosis is activated under phosphate starvation. This is attenuated upon deletion of an imperfect palindrome likely representing a binding site for the response regulator RegX3, a component of the two-component system SenX3-RegX3 that responds to phosphate starvation. The activity of the ppk1 promoter is abrogated upon deletion of a putative SigE binding site
additional information
-
the ppk1 promoter of Mycobacterium tuberculosis is activated under phosphate starvation. This is attenuated upon deletion of an imperfect palindrome likely representing a binding site for the response regulator RegX3, a component of the two-component system SenX3-RegX3 that responds to phosphate starvation. The activity of the ppk1 promoter is abrogated upon deletion of a putative SigE binding site
additional information
-
the ppk1 promoter of Mycobacterium tuberculosis is activated under phosphate starvation. This is attenuated upon deletion of an imperfect palindrome likely representing a binding site for the response regulator RegX3, a component of the two-component system SenX3-RegX3 that responds to phosphate starvation. The activity of the ppk1 promoter is abrogated upon deletion of a putative SigE binding site
-
additional information
-
downregulation of ppk1 leads to impaired survival of Mycobacterium tuberculosis in macrophages, the stringent response regulator ppGpp is impaired in the ppk1 knockout mutant and is restored after complementation with ppk1 of Mycobacterium tuberculosis, overview
-
additional information
-
PPK knockout organism is susceptible to oxidative stress
additional information
-
effect of oxidative and surface stress as well as anaerobiosis on the survival of a ppk1 knockout mutant PPK-KO, overview. Effect of inactivation of ppk1 on the transcription of mprA, mprB, sigE and rel, overview
additional information
-
PPK knockout organism is susceptible to oxidative stress
-
additional information
-
effect of oxidative and surface stress as well as anaerobiosis on the survival of a ppk1 knockout mutant PPK-KO, overview. Effect of inactivation of ppk1 on the transcription of mprA, mprB, sigE and rel, overview
-
additional information
-
PPK knockout organism is susceptible to oxidative stress
-
additional information
-
effect of oxidative and surface stress as well as anaerobiosis on the survival of a ppk1 knockout mutant PPK-KO, overview. Effect of inactivation of ppk1 on the transcription of mprA, mprB, sigE and rel, overview
-
additional information
construction of a ppk gene encoding the PPK insertional mutant in Proteus mirabilis strain HI4320
additional information
-
construction of a ppk gene encoding the PPK insertional mutant in Proteus mirabilis strain HI4320
-
additional information
-
ppk1 knockout organism, PAOM5, reveals profound deficiencies in cellular functions
additional information
Q9S646
ppk1 knockout organism, PAOM5, reveals profound deficiencies in cellular functions
additional information
-
the PPK1-deficient strain PAOM5, an isogenic mutant of strain PAO1, is significantly less virulent than either wild-type strain PAO1 or the complemented mutant, the loss of ocular virulence is probably due to the dysregulation of multiple genes, including those responsible for stress response, the PPK1-deficient mutant produces significantly less pyocyanin, phenotype, overview
additional information
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the ppk1 knockout mutant of Pseudomonas aeruginosa strain PAO1 exhibits multiple ultrastructural and functional defects, e.g. defects in motility, quorum sensing, biofilm formation, and virulence. It shows striking compaction of the nucleoid, distortion of the cell envelope, lack of planktonic motility and exopolymer production, and susceptibility to the beta-lactam antibiotic carbenicillin as well as desiccation, mutant cells fail to produce exopolymer, phenotype, overview
additional information
Q9S646
the ppk1 knockout mutant of Pseudomonas aeruginosa strain PAO1 exhibits multiple ultrastructural and functional defects, e.g. defects in motility, quorum sensing, biofilm formation, and virulence. It shows striking compaction of the nucleoid, distortion of the cell envelope, lack of planktonic motility and exopolymer production, and susceptibility to the beta-lactam antibiotic carbenicillin as well as desiccation, mutant cells fail to produce exopolymer, phenotype, overview
additional information
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construction of a truncated enzyme mutants comprising amino acid residues 1-314 of 506 (N-paPpx(1-314)), or residues 1-303 (N-paPpx(1-303)), or residues 315-506 (C-paPpx(315-506)) of paPpx, amplified from Pseudomonas aeruginosa wild-type strain PAO1 chromosomal DNA through PCR. Only paPpx(1-506) and N-paPpx(1-314) are enzymatically active, while C-paPpx(315-506) lacks enzymatic activity
additional information
genes ppk and ppx are adjacent to each other in the genome, a ppk-deficient mutant is more sensitive to oxidative stress than the wild-type and the ppx mutant, and shows reduced growth, phenotypes, overview
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complementation of the PPK1-deficient mutant strain PAOM5 by the wild-type PPK1
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Escherichia coli strain harboring plasmid pSPK5 with ppk gene increases enzyme activity of polyphosphate kinase, resulting in increased accumulation of polyphosphate in Escherichia coli
expressed in Enterobacter aerogenes IAM1183
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expressed in Enterobacter aerogenes strain IAM1183
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expressed in Escherichia coli BL-21 (DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Rosetta2 (DE3) pLysS cells
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expressed in Escherichia coli strain M15
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expressed in Escherichia coli strain NR 100
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expressed in Escherichia coli strains BL21 (DE3) and B834 (DE3)
expressed in Pseudomonas putida strain KT2440
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expressed in Streptomyces lividans
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expression in Escherichia coli
expression in Escherichia coli TOP10 cells
expression of His6-tagged Ppk in Escherichia coli strain BL21(DE3)
Thermosynechococcus vestitus
expression of polyphosphate kinase 2 gene in Escherichia coli
expression of type I polyphosphate kinase in Escherichia coli
expression with an N-terminal His-tag in Escherichia coli
gene Ddppk1, overexpression under control of the strong promoter Pact15, functional expression of GFP-DdPPK1 fusion protein
gene FTT1564, sequence comparisons, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21 Rosetta pLysS (DE3)
gene ppk, expression analysis
gene ppk, expression analysis, quantitative real-time PCR assay for polyphosphate kinase genes in activated sludge, method development and optimization, overview
Q9S646
gene ppk, quantitative expression analysis in wild-type and transfected recombinant cells, overview, expression in HEK-293 and HEK-293T cells, HeLa cells, Cos-7 cells
gene ppk, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene ppk, subcloning in Escherichia coli strain TOP10
gene ppk1, DNA and amino acid sequence determination and analysis, expression analysis in several different sludges, phylogenetic analysis
gene ppk1, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH10B, expression analysis, quantitative real-time PCR assay for polyphosphate kinase genes in activated sludge, method development and optimization, overview
gene ppk1, DNA and amino acid sequence determination and analysis, from at least five clades of Candidatus Accumulibacter, phylogenetic analysis
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59
gene ppk1, expression of wild-type and mutant enzymes
gene ppk1, the ppk1 promoter of Mycobacterium tuberculosis is activated under phosphate starvation, involvement of SigE in ppk1 transcription, binding of SigE to the ppk1 promoter. Quantitative RT-PCR ppk1 expression analysis. Gene ppk1 in vitro transcription
gene ppx, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strains XL10-Gold and BL21-CodonPlus
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gene SPO0224, DNA and amino acid sequence determination and analysis, recombinant expression of Strep-tagged isozyme PPK2-3 in Escherichia coli strain BL21(DE3)-T1
gene SPO1256, DNA and amino acid sequence determination and analysis, recombinant expression of STrep-tagged isoyzme PPK2-2 in Escherichia coli strain BL21(DE3)-T1
gene SPO1727, DNA and amino acid sequence determination and analysis, recombinant expression of Strep-tagged isozyme PPK2-1 in Escherichia coli strain BL21(DE3)-T1
genes NCgl0880 and NCgl2620 or pkk2A and pkk2B, expression of wild-type and mutant PKK2B isozymes in Escherichia coli strain Bl21(DE3), subcloning in Escherichia coli strain DH5alpha
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His-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
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overexpression in Escherichia coli
ppk1, DNA and amino acid sequence determination and analysis, recombinant expression of eYFP-tagged protein in Escherichia coli DELTAppk strain
ppk1b, DNA and amino acid sequence determination and analysis, recombinant expression of eYFP-tagged protein in Escherichia coli DELTAppk strain
ppk2a, DNA and amino acid sequence determination and analysis, recombinant expression of eYFP-tagged protein in Escherichia coli DELTAppk strain
ppk2b, DNA and amino acid sequence determination and analysis, recombinant expression of eYFP-tagged protein in Escherichia coli DELTAppk strain
ppk2c, DNA and amino acid sequence determination and analysis, recombinant expression of eYFP-tagged protein in Escherichia coli DELTAppk strain
ppk2d, DNA and amino acid sequence determination and analysis, recombinant expression of eYFP-tagged protein in Escherichia coli DELTAppk strain
ppk2e, DNA and amino acid sequence determination and analysis, recombinant expression of eYFP-tagged protein in Escherichia coli DELTAppk strain
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli strains BL21 (DE3) and B834 (DE3)
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expressed in Escherichia coli strains BL21 (DE3) and B834 (DE3)
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression in Escherichia coli
expression with an N-terminal His-tag in Escherichia coli
expression with an N-terminal His-tag in Escherichia coli
gene ppk1, expression of wild-type and mutant enzymes
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gene ppk1, expression of wild-type and mutant enzymes
overexpression in Escherichia coli
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overexpression in Escherichia coli
-
overexpression in Escherichia coli
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overexpression in Escherichia coli
Thermosynechococcus vestitus
overexpression in Escherichia coli
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industry
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copper polyphosphate kinase hybrid nanoflower (ArPPK2-Cu3(PO4)2·3H2O nanoflower) has an application potential in industrial catalytic processes that are coupled with ADP-dependent enzymes
molecular biology
A0MH70, A7XVX1, A7XVX6, A7XVX7, A7XVY1, A7XVY3, A7XVY6, A7XVY9, A7XVZ2, A7XVZ5, A7XVZ7, A7XVZ9, A7XW05, A7XW08, A7XW11, A7XW13, A7XW15, A7XW17, A7XW18, A7XW22, A7XW24, A7XW27, A7XW29, A7XW30, A7XW33, A7XW35, A7XW38, A7XW41, A7XW42, A7XW45, A7XW47, A7XW48, A7XW52, A7XW54, A7XW56, A7XW57, A7XW59 power of ppk1 as a genetic marker for detection of all currently defined Candidatus Accumulibacter clades
additional information
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enviromental protection, overexpression of polyP induces resistance to mercury, poly P in leaves mediates an accumulation of mercury from mercury-contaminated soil, phytoremediation of mercury pollution
analysis
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specific and sensitive assessment of polyphosphate in mycorrhizal system of Tagetes patula inoculated with Archaeospora leptoticha with a polyphosphate kinase/luciferase system
analysis
usage of polyphosphate kinase gene ppk1 as a high-resolution genetic marker to study population structure in activated sludge of Candidatus Accumulibacter phosphatis
analysis
usage of the gene ppk as reporter gene used in monitoring of gene expression in mammalian cells, method development involving 31P-magnetic resonance spectrocopy or 31P-resonance imaging, overview
analysis
enzyme-linked assay in which His-tagged PPK2 is immobilized on a plate and then biotinylated aptamer inhibitors are added
analysis
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enzyme-linked assay in which His-tagged PPK2 is immobilized on a plate and then biotinylated aptamer inhibitors are added
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biotechnology
Thermosynechococcus vestitus
ATP supply for synthesis of D-amino acid dipeptides
biotechnology
ATP supply for synthesis of D-amino acid dipeptides
biotechnology
polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
biotechnology
polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
biotechnology
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polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
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biotechnology
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ATP supply for synthesis of D-amino acid dipeptides
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biotechnology
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polyphosphate kinases use inexpensive and stable polyphosphate as a phosphate donor and phosphorylate nucleoside 5'-monophosphate as well as 5'-diphosphates. This makes them of special interest for application in ATP regeneration systems, which can be efficiently coupled to ATP-consuming enzymes in environmentally friendly and sustainable biotechnological processes
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drug development
Q9S646
enzyme PPK1 is an attractive therapeutic target to control infections caused by multiple drug resistant Pseudomonas aeruginosa
drug development
the enzym eis a target for inhibitor development
drug development
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the enzyme might be a potential drug target in bacteria
drug development
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the enzyme might be a potential drug target in bacteria
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environmental protection
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bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in Escherichia coli. Specific application of this process to polyphosphate is of potential application for biological phosphate removal
environmental protection
E245K mutation leads to very high polyphosphate accumulation in vivo but is not different from the wild type in either activity or chain length of polyphosphate produced in vitro. Polyphosphate accumulation by bacteria is important in biotechnology applications, e.g. to enhanced biological phosphate removal (EBPR) from wastewater
environmental protection
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E245K mutation leads to very high polyphosphate accumulation in vivo but is not different from the wild type in either activity or chain length of polyphosphate produced in vitro. Polyphosphate accumulation by bacteria is important in biotechnology applications, e.g. to enhanced biological phosphate removal (EBPR) from wastewater
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medicine
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PPK1 is necessary for survival under anaerobic conditions or oxidative stress
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
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PPK1 exhibits potential as a target for chemotherapy
medicine
-
PPK1 exhibits potential as a target for chemotherapy
medicine
-
PPK1 exhibits potential as a target for chemotherapy
medicine
-
PPK1 exhibits potential as a target for chemotherapy
medicine
-
PPK1 exhibits potential as a target for chemotherapy
medicine
PPK1 exhibits potential as a target for chemotherapy
medicine
-
PPK1 is necessary for survival under anaerobic conditions or oxidative stress
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medicine
-
PPK1 is necessary for survival under anaerobic conditions or oxidative stress
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synthesis
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synthesis
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used for an ATP regeneration system for acetyl-CoA synthesis
synthesis
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used in place of pyruvate kinase and phosphoenol pyruvate for NTP regeneration followed by synthesis of sugar nucleotides in a cyclic synthesis system for oligosaccharides
synthesis
Thermosynechococcus vestitus
the enzyme is used to establih a thermostable ATP regeneration system from polyphosphate substrate, this is then used for synthesis of D-Ala-D-Ala in a coupled system with the thermostable D-alanine-D-alanine ligase TmDdl from Thermotoga maritima, a useful biocatalyst for synthesizing D-amino acid dipeptides, method development and optimization, overview
synthesis
the enzyme is useful for ATP production from polyphosphate
synthesis
a biocatalytic cascade of polyphosphate kinase and sucrose synthase is developed for synthesis of nucleotide-activated derivatives of glucose
synthesis
a biocatalytic cascade of polyphosphate kinase and sucrose synthase is developed for synthesis of nucleotide-activated derivatives of glucose
synthesis
construction of an ATP regeneration system from AMP using PPK2, coupled with aminoacyl proline (Xaa-Pro) synthesis catalyzed by the adenylation domain of tyrocidine synthetase TycA-A. 0.87 mM of L-Trp-L-Pro is successfully synthesized from AMP after 72 h. Addition of inorganic diphosphatase increases the reaction rate by 14fold. When the coupling reaction is applied to whole-cell reactions in Escherichia coli, ATP is successfully regenerated from AMP, and 6.7 mM of L-Trp-L-Pro is produced after 24 h with the supplementation of 10 mM AMP. Also various other L-Xaa-L-Pro an be produced
synthesis
ANU33171.1
efficient synthesis of gamma-glutamyl compounds by co-expression of gamma-glutamylmethylamide synthetase and polyphosphate kinase in engineered Escherichia coli
synthesis
energy delivery is a critical aspect of cell-free protein synthesis. The single kinase-based regeneration system simplifies cell free protein synthesis from a three-kinase system to single-kinase system, and potentially cheapens the cost of reagent preparations by using polyP instead of phosphocreatine. Incorporation of the PPK2-based NTP regeneration system into synthetic biomembrane vesicles can lead to artificial cell and proto-cell systems more akin to their natural counterparts
synthesis
enzymatic production of glutathione coupling with an ATP regeneration system based on polyphosphate kinase
synthesis
potential application for ATP regeneration in cascade reaction
synthesis
potential application for ATP regeneration in cascade reaction
synthesis
PPK2 is used for ATP regeneration to produce glutathione by a two-enzyme cascade in vitro. 47.1 mM glutathione can be synthesized with a productivity of 13.5 mM/h. ATP is regenerated approximately 471 times in the system within 3.5 h
synthesis
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potential application for ATP regeneration in cascade reaction
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synthesis
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PPK2 is used for ATP regeneration to produce glutathione by a two-enzyme cascade in vitro. 47.1 mM glutathione can be synthesized with a productivity of 13.5 mM/h. ATP is regenerated approximately 471 times in the system within 3.5 h
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synthesis
-
the enzyme is useful for ATP production from polyphosphate
-
synthesis
-
enzymatic production of glutathione coupling with an ATP regeneration system based on polyphosphate kinase
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synthesis
-
construction of an ATP regeneration system from AMP using PPK2, coupled with aminoacyl proline (Xaa-Pro) synthesis catalyzed by the adenylation domain of tyrocidine synthetase TycA-A. 0.87 mM of L-Trp-L-Pro is successfully synthesized from AMP after 72 h. Addition of inorganic diphosphatase increases the reaction rate by 14fold. When the coupling reaction is applied to whole-cell reactions in Escherichia coli, ATP is successfully regenerated from AMP, and 6.7 mM of L-Trp-L-Pro is produced after 24 h with the supplementation of 10 mM AMP. Also various other L-Xaa-L-Pro an be produced
-
synthesis
-
a biocatalytic cascade of polyphosphate kinase and sucrose synthase is developed for synthesis of nucleotide-activated derivatives of glucose
-
synthesis
-
potential application for ATP regeneration in cascade reaction
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