2.7.4.1: ATP-polyphosphate phosphotransferase
This is an abbreviated version!
For detailed information about ATP-polyphosphate phosphotransferase, go to the full flat file.
Word Map on EC 2.7.4.1
-
2.7.4.1
-
phosphorus
-
exopolyphosphatase
-
molecular biology
-
wastewater
-
sludge
-
polyhydroxyalkanoates
-
accumulibacter
-
candidatus
-
synthesis
-
polyphosphatase
-
medicine
-
phosphoanhydride
-
phosphatis
-
biotechnology
-
drug development
-
analysis
-
industry
-
environmental protection
- 2.7.4.1
- phosphorus
- exopolyphosphatase
- molecular biology
-
wastewater
- sludge
- polyhydroxyalkanoates
- accumulibacter
-
candidatus
- synthesis
- polyphosphatase
- medicine
-
phosphoanhydride
- phosphatis
- biotechnology
- drug development
- analysis
- industry
- environmental protection
Reaction
Synonyms
AAur2811, AjPPK, ATP:polyphosphate phosphotransferase, AUJ86_09545, CHU0107, CHU_0107, class I PPK2, class II polyphosphate kinase, class III PPK2, Deipr_1912, DR0132, DR_0132, ES2, family-2 polyphosphate kinase, FTT_1564, glycogen-bound polyphosphate kinase, GmSuSy, I601_4057, K649_10090, kinase, polyphosphate (phosphorylating), More, MrH2468, Mrub_2488, MXAN_0056, NCg12620, OsIPK2, PA0141, PA3455 protein, paPpx, plyphosphate kinase 1, poly P kinase 1, poly(P) kinase 1, poly(P) kinase 2, poly-P kinase, poly-P kinase 1, polyP kinase, polyphosphate kinase, polyphosphate kinase 1, polyphosphate kinase 2, polyphosphate kinase 3, polyphosphate kinase-1, polyphosphate kinase-2, polyphosphate-dependent nucleoside diphosphate kinase, polyphosphate: ADP phosphotransferase, polyphosphate:ADP phosphotransferase, polyphosphate:nucleotide phosphotransferase, polyphosphoric acid kinase, PPK, PPK-2, PPK1, PPK2, PPK2-1, PPK2-2, PPK2-3, PPK2a, PPK2B, PPK2c, PPK2d, PPK2e, PPK3, Rv3232c, SMc02148, SMc02148 protein, SPO0224, SPO1256, SPO1727
ECTree
2.7.4.1 ATP-polyphosphate phosphotransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.7.4.1 - ATP-polyphosphate phosphotransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ADP + phosphate(6)
ATP + phosphate(5)
ANU33171.1
i.e. hexametaphosphate
-
-
?
ATP + (phosphate)n+1
ADP + (phosphate)n
-
-
-
r
ATP + ATP
ADP + (phosphate)n+1
-
polyP not required as primer
-
-
r
GDP + (phosphate)20
GTP + (phosphate)19
-
isoform PPK1 affinity for the ADP as a substrate is about 70fold high as opposed to GDP
-
-
r
GTP + (phosphate)n+1
GDP + (phosphate)n
-
-
-
r
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)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)n
ATP + (phosphate)n-1
-
-
-
r
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+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
-
-
-
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
enzyme prefers polyphosphate of 25 to 50 in chain length
-
-
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
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
-
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
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
the enzyme preferentially catalyzes the long-chain polyP hexametaphosphate as the phosphate donor. No activity with AMP
-
-
?
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
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
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
polyphosphate kinases (PPKs) catalyzes the polyP formation or ATP formation, to store energy or to regenerate ATP, respectively
-
-
r
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)n+2
ATP + (phosphate)n
-
-
-
r
AMP + (phosphate)n+2
ATP + (phosphate)n
-
-
-
r
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
-
no activity with CTP, GTP and TTP
-
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
-
-
-
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
-
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
-
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
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
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
-
-
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
Escherichia coli B / ATCC 11303
-
phosphate polymers act as templates for polyphosphate synthesis, e.g. tetrapolyphosphate, trimetaphosphate or tetrametaphosphate
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
-
-
-
r
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
-
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
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
-
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
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
-
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
-
-
-
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
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
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
-
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
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
-
glycogen-bound polyphosphate kinase
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
-
the enzyme does not require the presence of histones for its activity
-
-
?
CDP + (phosphate)n
CTP + (phosphate)n-1
-
-
-
?
CDP + (phosphate)n+1
CTP + (phosphate)n
-
the efficiency of polyphosphate utilization by PKK3 is 100%
-
-
?
dADP + (phosphate)n+1
dATP + (phosphate)n
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
-
-
-
r
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
-
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
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
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
-
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
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
-
lower activity compared to ATP
-
-
r
UDP + (phosphate)n
UTP + (phosphate)n-1
-
-
-
?
[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
?
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enzyme additionally displays adenylate kinase activity in both reaction directions
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additional information
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Francisella tularensis Schu 4
enzyme additionally displays adenylate kinase activity in both reaction directions
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additional information
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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
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additional information
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enzyme also accepts GDP, reaction of Ec 2.7.4.34. No substrates: CDP, UDP
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additional information
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enzyme preferentially accepts hexametaphosphate as the phosphate donor. No substrates: diphosphate or triphosphate, and AMP
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additional information
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enzyme preferentially accepts hexametaphosphate as the phosphate donor. No substrates: diphosphate or triphosphate, and AMP
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additional information
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enzyme preferentially accepts hexametaphosphate as the phosphate donor. No substrates: diphosphate or triphosphate, and AMP
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additional information
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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
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additional information
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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
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additional information
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enzyme additionally displays adenylate kinase activity in both reaction directions
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additional information
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enzyme is able to use nucleoside diphosphates ADP, GDP, CDP, and UDP
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additional information
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enzyme additionally displays adenylate kinase activity in both reaction directions
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additional information
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enzyme is able to use nucleoside diphosphates ADP, GDP, CDP, and UDP
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additional information
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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
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additional information
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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
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additional information
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PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
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additional information
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the enzyme is unable to use triphosphate or pentaphosphate as phosphate donors
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additional information
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the enzyme is unable to use triphosphate or pentaphosphate as phosphate donors
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additional information
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PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
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additional information
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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
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additional information
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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
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additional information
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PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
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additional information
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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
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additional information
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Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
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additional information
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Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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enzyme preferentially accepts hexametaphosphate as the phosphate donor. No or poor substrates: diphosphate or triphosphate, and AMP
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additional information
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enzyme preferentially accepts hexametaphosphate as the phosphate donor. No or poor substrates: diphosphate or triphosphate, and AMP
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additional information
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enzyme preferentially accepts hexametaphosphate as the phosphate donor. No or poor substrates: diphosphate or triphosphate, and AMP
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additional information
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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
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additional information
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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
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additional information
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GTP (reaction of EC 2.7.4.34) and ATP are equally active in polyphosphate synthesis
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additional information
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GTP (reaction of EC 2.7.4.34) and ATP are equally active in polyphosphate synthesis
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additional information
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GTP (reaction of EC 2.7.4.34) and ATP are equally active in polyphosphate synthesis
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additional information
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gene ppk regulates the transcription accumulation of the stationary-phase sigma factor RpoS encoded by the rpoS gene, overview
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additional information
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all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
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additional information
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all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
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additional information
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all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
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additional information
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all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
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additional information
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all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
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additional information
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all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
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additional information
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all PPK isozymes from Ruegeria pomeroyi accept all NDPs similarly and exhibit low NDP selectivity
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additional information
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enzyme additionally displays adenylate kinase activity in both reaction directions
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additional information
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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
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additional information
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production of choline from hydrolysis of 1,2-dioleoyl-sn-glycero-3-phosphocholine in the presence of the Amplex Red reagent by enzyme PPK
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