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Enzyme Nomenclature
Information on EC 2.7.4.1 - polyphosphate kinase
for references in articles please use BRENDA:EC2.7.4.1
Word Map on EC 2.7.4.1
- 2.7.4.1
- phosphorus
- exopolyphosphatase
- molecular biology
-
wastewater
-
sludge
-
polyhydroxyalkanoates
- accumulibacter
- polyphosphatase
- medicine
-
candidatus
-
phosphoanhydride
- synthesis
- analysis
- drug development
- biotechnology
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
2.7.4.1
-
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RECOMMENDED NAME
GeneOntology No.
polyphosphate kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (phosphate)n = ADP + (phosphate)n+1
-
-
-
-
ATP + (phosphate)n = ADP + (phosphate)n+1
short chain polyphosphates are incorporated at the ends of the long chain product
-
ATP + (phosphate)n = ADP + (phosphate)n+1
both polyphosphate synthesis and polyphosphate utilization follow a processive mechanism; mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:polyphosphate phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9026-44-2
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MH20-22B; wild-type strain ATCC 13032 is auxotrophic for biotin, genes NCgl0880 and NCgl2620 encoding class II isozymes PPK2A and PPK2B, no class I polyphosphate kinase, PPK1, encoded by ppk1, in this bacterium
-
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
an extraintestinal pathogenic Escherichia coli strain ExPEC, gene ppk
UniProt
stibogluconate-resistant and paromomycin-resistant clone AG83
-
-
Mycobacterium smegmatis mc(2)155 / ATCC 700084
T3 progeny of ppk-transgenic tabacum, engineered to express bacterial PPK1
-
-
Rhodocyclus-like beta-Proteobacteria enriched in activating sludge carrying out enhanced biological phosphorus removal
SwissProt
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
i.e. Cupriavidus necator, gene ppk1 or H16_A2437
UniProt
-
645111, 645113, 645115, 645116, 645125, 645126, 645127, 645129, 645130, 645134, 662905, 662964, 721876, 722321
-
-
an extraintestinal pathogenic Escherichia coli strain ExPEC, gene ppk
UniProt
gene ppk1, strains MPAO1 and ppk1 mutant PW9825, and clinical strains (P1-P11) from burn and sepsis patients
Q9S646
SwissProt
fragment; uncultured bacterium named Candidatus Accumulibacter Phosphatis, genes ppk1 and ppk2, encoding two isozymes PPK1 and PPK2
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
UniProt
PPK1; uncultured bacterium named Candidatus Accumulibacter Phosphatis,gene ppk1
UniProt
uncultured bacterium named Candidatus Accumulibacter phosphatis, gene ppk1
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
a lid-loop and the conserved Walker A and B motifs are important for substrate binding and enyzme catalysis
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; 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; 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; 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; 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
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malfunction
-
mutants lacking PPK1 are defective in motility, quorum sensing, biofilm formation, and virulence
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
-
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
-
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
-
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
-
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
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
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 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
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
-
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
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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
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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
-
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
-
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 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
-
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)
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metabolism
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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; 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; 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; 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; 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; 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; 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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
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; 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; 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; 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; 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; 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; 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
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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
important role for polyphosphate in the virulence of Francisella
physiological function
enzyme PPK is important for the antibiotic stress response during the planktonic growth of extraintestinal pathogenic Escherichia coli
physiological function
-
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
physiological function
Q9S646
polyphosphate kinase 1 plays an important role in virulence, antibiotic resistance and survival under stress conditions
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
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
-
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
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physiological function
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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
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physiological function
-
enzyme PPK is important for the antibiotic stress response during the planktonic growth of extraintestinal pathogenic Escherichia coli
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physiological function
-
substrate level phosphorylation is essential for the survival of amastigote forms of Leishmania donovani
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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
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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
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physiological function
-
polyphosphate kinase is necessary for optimal competitive fitness in LB broth culture and sterile loam soil
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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
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)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
not (phosphate)3, (phosphate)4 as preferred phosphate donor
-
-
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
-
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
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
-
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
-
-
?
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
-
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
-
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
-
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
-
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, 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
-
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%
-
-
?
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
Mycobacterium 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
-
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
-
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
-
-
-
?
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
?
-
-
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
?
-
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
?
-
-
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
?
-
-
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
?
-
Mycobacterium smegmatis mc(2)155 / ATCC 700084
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
-
additional information
?
-
Mycobacterium smegmatis mc(2)155 / ATCC 700084
-
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
?
-
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
?
-
-
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
?
-
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
?
-
-
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
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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)n
ATP + (phosphate)n-1
Q5NEQ5
-
-
-
r
ADP + (phosphate)n
ATP + (phosphate)n-1
Q5LSN8, Q5LU04, Q5LX16
-
-
-
?
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
P0DP45
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
P0DP45
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
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
A1W0X7
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
A1W0X7
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
-
PPK2B forms polyphopshate with an average chain length of about 125
-
-
r
ATP + (phosphate)n
ADP + (phosphate)n+1
Q0K2G4, Q0K8Z5, Q0KA91, Q0KC60, Q0KCB8, Q0KCY1, Q0KF43
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
Q0K2G4, Q0K8Z5, Q0KA91, Q0KC60, Q0KCB8, Q0KCY1, Q0KF43
-
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Q54BM7
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 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
-
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
-
PPK1 is essential for a successful ocular infection by the organism
-
-
?
ATP + (phosphate)n
ADP + (phosphate)n+1
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
Q72JY1
-
-
-
r
CDP + (phosphate)n
CTP + (phosphate)n-1
Q5LSN8, Q5LU04, Q5LX16
-
-
-
?
GDP + (phosphate)n
GTP + (phosphate)n-1
Q5LSN8, Q5LU04, Q5LX16
-
-
-
?
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
Q5LSN8, Q5LU04, Q5LX16
-
-
-
?
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
?
-
Q54BM7
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, 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
?
-
Mycobacterium smegmatis mc(2)155 / ATCC 700084
-
PPK2 interacts with and modulates nucleotide-synthesizing activity of nucleoside diphosphate kinase
-
-
-
additional information
?
-
Mycobacterium smegmatis mc(2)155 / ATCC 700084
-
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
?
-
P9WHV9
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
?
-
P9WHV9
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
?
-
Q209Q9
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
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
1.5-2.5fold lower activation than with Mg2+, inhibitory with Mg2+ as activator
KCl
Mg2+
Mn2+
Zn2+
additional information
KCl
Dictyostelium discoideum also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
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+
; 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+
-
active substrate: MgATP; inhibitory above 6 mM; required for activity
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+
Mn2+
-
1.5-2.5fold lower activation than with Mg2+; activation, can replace Mg2+
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+
-
activation, can replace Mg2+; active substrate: MnATP; maximal activity at 1.0-2.0 mM, inhibition above 2 mM
additional information
lower optimal concentration for Mn2+ ions than Mg2+ ions
additional information
-
Fe2+, Zn2+, Cu2+ cannot be used by the enzyme
additional information
enzyme SPO1727 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview; isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview; isozyme SPO125 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; isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview; isozyme SPO125 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; isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview; isozyme SPO125 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; isozyme SPO0224 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview; isozyme SPO125 requires a divalent cation, but shows no specificity, only Co2+ is not accepted, overview
additional information
-
not activated by NH4Cl
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
histone
-
reverse reaction, strong, activates forward reaction in the presence of phosphate
NH4Cl
-
200 mM, approx. 50% inhibition of glycogen-bound polyphosphate kinase
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
(NH4)2SO4
-
activation up to 100 mM; inhibition at higher concentrations; 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
-
50%, 70% and 93% inhibition at 0.08 mM, 0.15 mM and 0.2 mM ADP, respectively
ADP
-
0.25 mM, approx. 50% inhibition, 1 mM, complete inhibition
ADP
-
2 mM, 50% inhibition of glycogen-bound polyphosphate kinase; product inhibition, about 50% inhibition at 2 mM
AMP
-
15% and 70% inhibition of the forward reaction at AMP/ADP ratios of 1 and 10, respectiverly
Co2+
complete inhibition; complete inhibition; complete inhibition
diphosphate
-
10 mM, 66% inhibition of polyphosphate synthesis, 75% inhibition of GTP synthesis
GMP
-
competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
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 inhbition
Polyphosphate
-
65 residues, competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
additional information
-
not inhibited by 2,4-dinitrophenol or potassium arsenate
-
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
-
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
-
a G9-quadruplex DNA aptamer inhibits isoform PPK2 with an IC50 of 105 nM and exhibits noncompetitive inhibition kinetics
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
actin
Dictyostelium discoideum also has an actin-related poly P synthesizing complex, DdPPK2, that is KCl dependent
diphosphate
-
10 mM, 100% activation of guanosine 5'-tetraphosphate synthesis
Guanidine HCl
-
5 mM, 20% activation of guanosine 5'-tetraphosphate synthesis
Tetrapolyphosphate
-
activation, removes lag-phase in synthesis at low ATP-levels, not phosphate, diphosphate or tripolyphosphate
bovine serum albumin
-
activation, can substitute for histone only in the absence of phosphate
-
bovine serum albumin
-
activation, can substitute for histone only in the absence of phosphate
-
casein
-
activation, can substitute for histone only in the absence of phosphate
casein
-
activation, can substitute for histone only in the absence of phosphate
histone
-
maximum activation in the presence of 20 mM phosphate; strong inhibition of reverse reaction
phosphate
-
inhibiton above 20 mM; required for activity, only in the presence of histone
phosphate
-
10fold higher rate of polyphosphate synthesis
additional information
-
polyphosphate or ATP promote oligomerization of the enzyme in vitro, polyphosphate activates about 10fold
-
additional information
polyphosphate or ATP promote oligomerization of the enzyme in vitro, polyphosphate activates about 10fold
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
0.1
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
-
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
2
ADP
-
mutant Y524A of isoform PPK1, pH and 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
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
1.35
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
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
11.3
GDP
-
isoform PPK1, pH and temperature not specified in the publication
additional information
additional information
-
exponential kinetics
-
additional information
additional information
Michalis-Menten steady state kinetic analysis of FtPPK2 substrate specificity, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
-
210
ADP
-
isoform PPK2, 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
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
645
GDP
-
isoform PPK1, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
3.704
(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
-
25.5
ADP
-
isoform PPK2, pH and temperature not specified in the publication
49
ADP
-
mutant H510A of isoform PPK1, pH and temperature not specified in the publication
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
4.2
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
57
GDP
-
isoform PPK1, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.9
AMP
-
no inhibition by CMP and UMP; pH 7.2, 30°C, recombinant wild-type enzyme
0.0007
GMP
-
pH 7.5, 37°C, competitive inhibition of GDP in guanosine 5'-tetraphosphate synthesis
0.0014
GMP
-
pH 7.5, 37°C, competitive inhibition of polyphosphate 750 in guanosine 5'-tetraphosphate synthesis
0.0012
polyphosphate 65
-
pH 7.5, 37°C, competitive inhibition of GDP in guanosine 5'-tetraphosphate synthesis
-
0.0076
polyphosphate 65
-
pH 7.5, 37°C, competitive inhibition of polyphosphate 750 in guanosine 5'-tetraphosphate synthesis
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE