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Information on EC 2.7.4.1 - ATP-polyphosphate phosphotransferase and Organism(s) Escherichia coli and UniProt Accession P0A7B1
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2.7.4.1 ATP-polyphosphate phosphotransferaseIUBMB Comments
The enzyme is responsible for the synthesis of most of the cellular polyphosphate, using the terminal phosphate of ATP as substrate.
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Word Map
- 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
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
polyphosphate kinase, polyphosphate kinase 1, polyp kinase, polyphosphate kinase 2, ppk-2, class iii ppk2, ppk2b, ppk2c, poly p kinase 1, osipk2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kinase, polyphosphate (phosphorylating)
-
-
-
-
polyphosphate kinase 1
PPK
PPK1
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:polyphosphate phosphotransferase
The enzyme is responsible for the synthesis of most of the cellular polyphosphate, using the terminal phosphate of ATP as substrate.
CAS REGISTRY NUMBER
COMMENTARY
9026-44-2
-
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)n+1
ATP + (phosphate)n
-
polyphosphate kinase directly or indirectly regulates DNA polymerase activity or fidelity
-
-
?
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
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+2
guanosine 5'-tetraphosphate + (phosphate)n
-
-
-
?
GDP + (phosphate)n+2
guanosine 5'-tetraphosphate + (phosphate)n
-
diphosphate group transfer
-
ir
NATURAL SUBSTRATE
NATURAL 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)n+1
ATP + (phosphate)n
-
polyphosphate kinase directly or indirectly regulates DNA polymerase activity or fidelity
-
-
?
GDP + (phosphate)n+1
GTP + (phosphate)n
-
efficiency of NDP substrates in descending order: ADP, dADP, dGDP, GDP, TDP, UDP, CDP, dCDP
-
ir
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
1.5-2.5fold lower activation than with Mg2+, inhibitory with Mg2+ as activator
Mg2+
Mn2+
additional information
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-[2-amino-3-[(2-amino-3-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-3-oxopropyl)disulfanyl]propanamido]-3-(4-hydroxyphenyl)propanoic acid
treating the wild-type Escherichia coli with the inhibitor, at 0.050 mM, results in a metabolic fingerprint that is an almost identicalntical metabolic behavior to the ppk1 knockout mutant
6-(4-aminobenzamido)-5-[(E)-[1-(2-chloro-5-sulfophenyl)-5-hydroxy-3-methyl-1H-pyrazol-4-yl]diazenyl]naphthalene-2-sulfonic acid
treating the wild-type Escherichia coli with the inhibitor, at 0.050 mM, results in a metabolic fingerprint that is completely identical to that of ppk1 knockout mutant
GMP
-
competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
histone
-
reverse reaction, strong, activates forward reaction in the presence of phosphate
Polyphosphate
-
65 residues, competitive inhibition of polyphosphate 750 and GDP in guanosine 5'-tetraphosphate synthesis
threonyltyrosyl-N-[(1R)-1-[(3-aminopropyl)amino]-2-(carboxyoxy)-2-oxoethyl]serinamide
poor chemical inhibitor of PPK1, it shows a drop of approximately 20% in the WT biofilm formation ability
[2-(2,3-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
-
[2-[(1-amino-2-methylbutyl)(hydroxy)phosphoryl]ethyl]phosphonic acid
-
ADP
-
50%, 70% and 93% inhibition at 0.08 mM, 0.15 mM and 0.2 mM ADP, respectively
diphosphate
-
10 mM, 66% inhibition of polyphosphate synthesis, 75% inhibition of GTP 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
screening of low-molecular-weight organophosphorus inhibitors against polyphosphate kinases from Cytophaga hutchinsonii and Escherichia coli. For Escherichia coli PPK1, only individual compounds with a distinct scaffold and functional group arrangement show potency
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.064
(2-anilinoethane-1,1-diyl)bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.752
(2E)-2-[(4-nitrophenyl)methylidene]-4,4-diphosphonobutanoic acid
Escherichia coli
pH 8, temperature not specified in the publication
0.103
[(3-aminoanilino)methylene]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.468
[(3-carbamimidamidoanilino)methylene]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.645
[2-(2,3-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.058
[2-(3,4-dichlorophenyl)-1-hydroxyethane-1,1-diyl]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
0.935
[2-(3-chloroanilino)ethane-1,1-diyl]bis(phosphonic acid)
Escherichia coli
pH 8, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 8.2
-
approx. 45% of maximal activity at pH 6.2, approx. 75% of maximal activity at pH 8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
crude membrane fractions contain virtually all the polyphosphate kinase activity catalyzing the synthesis of ATP from ADP and polyphosphate
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
-
cell growth, hydrogen productivity and cellular metabolism of Enterobacter aerogenes IAM1183 are affected by the external addition of diphosphate and the overexpression of the enzyme at different initial glucose concentrations
physiological function
drug target
bacterial species, including many pathogens, encode a homolog of a major polyP synthesis enzyme, polyphosphate kinase (PPK) with 2 different genes coding for PPK1 and PPK2. Genetic deletion of the ppk1 gene leads to reduced polyP levels and the consequent loss of virulence and stress adaptation responses. No PPK1 homolog has been identified in higher-order eukaryotes, and, therefore, PPK1 represents a target for chemotherapy
drug target
-
the absence of a polyphosphate kinase orthologue in humans makes it a potential drug target
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
a mutant lacking the enzyme (PPK) makes no detectable polyP under any condition
malfunction
gene deletion alters specific metabolic pathways, changing the metabolic fingerprint, and suppressing the ability of Escherichia coli to form a biofilm
malfunction
-
polyphosphate kinase deletion increases sensitivity to H2O2 and reduces polyphosphate accumulation. Polyphosphate kinase deletion upregulates fermentation, aerobic and anaerobic respiration, enhances catalase and Clp protease activity, down-regulates ATP-dependent RNA helicase, DNA polymerase III and pyruvate kinase I
malfunction
-
polyphosphate kinase ppk1 deletion causes poor survival during osmotic shock and acid challenge
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
-
enzyme PPK is important for the antibiotic stress response during the planktonic growth of extraintestinal pathogenic Escherichia coli
physiological function
-
in Escherichia coli polyphosphate levels are controlled via the polyphosphate-synthesizing enzyme polyphosphate kinase (PPK1) and exopolyphosphatases (PPX and GPPA), and are temporarily enhanced by PPK1 overexpression and reduced by PPX overexpression
physiological function
-
the enzyme has wide distribution among pathogens and is involved in promoting pathogenesis, stress management and susceptibility to antibiotics
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
autophosphorylation using polyphosphate as phospho-donor
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
full-length polyphosphate kinase and its complex with beta-gamma-imidoadenosine 5-phosphate
hanging drop vapor diffusion method at room temperatur, long rod crystals appear after 3 days in a mixture of 0.005 ml protein and 0.005 ml reservoir solution consisting of 12-14% hexandiol, 10 mM dithiothreitol, 100 mM Tris-HCl, pH 7.5, crystals of polyphosphate kinase complexed with AMP-PNP diffract to 2.5 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D230N
the variant has somewhat greater processivity than the wild-type enzyme
E173K
the variant has somewhat greater processivity than the wild-type enzyme
E245K
mutation leads to very high polyP accumulation in vivo but is not different from the wild type in either activity or chain length of polyP produced in vitro
Y468A
-
120-140% of wild-type polyphosphate, GTP, and guanosine 5'-tetraphosphate synthesis activity, 20-50% of wild-type ATP synthesis activity
additional information
-
generation of a ppk knockout mutant strain, DELTAppk
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
specific and sensitive assessment of polyphosphate in mycorrhizal system of Tagetes patula inoculated with Archaeospora leptoticha with a polyphosphate kinase/luciferase system
environmental protection
synthesis
environmental protection
-
bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in Escherichia coli. Specific application of this process to polyphosphate is of potential application for biological phosphate removal
environmental protection
E245K mutation leads to very high polyphosphate accumulation in vivo but is not different from the wild type in either activity or chain length of polyphosphate produced in vitro. Polyphosphate accumulation by bacteria is important in biotechnology applications, e.g. to enhanced biological phosphate removal (EBPR) from wastewater
synthesis
-
used in place of pyruvate kinase and phosphoenol pyruvate for NTP regeneration followed by synthesis of sugar nucleotides in a cyclic synthesis system for oligosaccharides
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kornberg, A.; Kornberg, S.R.; Simms, E.S.
metaphosphate synthesis by an enzyme from Escherichia coli
Biochim. Biophys. Acta
20
215-227
1956
Escherichia coli
Murata, K.; Uchida, T.; Kato, J.; Chibata, I.
Polyphosphate kinase: distribution, some properties and its applicatin as an ATP regeneration system
Agric. Biol. Chem.
52
1471-1477
1988
Achromobacter butyri, Alcaligenes faecalis, Bacillus subtilis, Clavibacter michiganensis subsp. sepedonicus, Corynebacterium ammoniagenes, Escherichia coli, Escherichia coli B / ATCC 11303, Klebsiella aerogenes, Komagataeibacter xylinus, Micrococcus flavus, Micrococcus luteus, Pseudomonas aeruginosa, Sinomonas atrocyanea, [Brevibacterium] flavum
-
Li, H.C.; Brown, G.G.
Orthophosphate and histone dependent polyphosphate kinase from E. coli
Biochem. Biophys. Res. Commun.
53
875-881
1973
Escherichia coli
Ahn, K.; Kornberg, A.
Polyphosphate kinase from Escherichia coli. Purification and demonstration of a phosphoenzyme intermediate
J. Biol. Chem.
265
11734-11739
1990
Escherichia coli
Haeusler, P.A.; Dieter, L.; Rittle, K.J.; Shepler, L.S.; Paszkowski, A.L.; Moe, O.A.
Catalytic properties of Escherichia coli polyphosphate kinase: an enzyme for ATP regeneration
Biotechnol. Appl. Biochem.
15
125-133
1992
Escherichia coli
Kuroda, A.; Kornberg, A.
Polyphosphate kinase as a nucleoside diphosphate kinase in Escherichia coli and Pseudomonas aeruginosa
Proc. Natl. Acad. Sci. USA
94
439-442
1997
Escherichia coli, Pseudomonas aeruginosa
Noguchi, T.; Shiba, T.
Use of Escherichia coli polyphosphate kinase for oligosaccharide synthesis
Biosci. Biotechnol. Biochem.
62
1594-1596
1998
Escherichia coli
Shiba, T.; Tsutsumi, K.; Ishige, K.; Noguchi, T.
Inorganic polyphosphate and polyphosphate kinase: their novel biological functions and applications
Biochemistry
65
315-323
2000
Escherichia coli
Tzeng, C.M.; Kornberg, A.
The multiple activities of polyphosphate kinase of Escherichia coli and their subunit structure determined by radiation target analysis
J. Biol. Chem.
275
3977-3983
2000
Escherichia coli
Kameda, A.; Shiba, T.; Kawazoe, Y.; Satoh, Y.; Ihara, Y.; Munekata, M.; Ishige, K.; Noguchi, T.
A novel ATP regeneration system using polyphosphate-AMP phosphotransferase and polyphosphate kinase
J. Biosci. Bioeng.
91
557-563
2001
Escherichia coli
Zhu, Y.; Lee, S.S.; Xu, W.
Crystallization and characterization of polyphosphate kinase from Escherichia coli
Biochem. Biophys. Res. Commun.
305
997-1001
2003
Escherichia coli
Zhu, Y.; Huang, W.; Lee, S.S.; Xu, W.
Crystal structure of a polyphosphate kinase and its implications for polyphosphate synthesis
EMBO Rep.
6
681-687
2005
Escherichia coli (P0A7B1), Escherichia coli
Stumpf, J.D.; Foster, P.L.
Polyphosphate kinase regulates error-prone replication by DNA polymerase IV in Escherichia coli
Mol. Microbiol.
57
751-761
2005
Escherichia coli
Ezawa, T.; Cavagnaro, T.R.; Smith, S.E.; Smith, F.A.; Ohtomo, R.
Rapid accumulation of polyphosphate in extraradical hyphae of an arbuscular mycorrhizal fungus as revealed by histochemistry and a polyphosphate kinase/luciferase system
New Phytol.
161
387-392
2004
Escherichia coli
Brown, M.R.; Kornberg, A.
The long and short of it - polyphosphate, PPK and bacterial survival
Trends Biochem. Sci.
33
284-290
2008
Klebsiella aerogenes, Bacillus anthracis, Bacillus cereus, Dictyostelium discoideum, Helicobacter pylori, Myxococcus xanthus, Neisseria meningitidis, Pseudomonas aeruginosa, Escherichia coli (P0A7B1)
Hooley, P.; Whitehead, M.P.; Brown, M.R.
Eukaryote polyphosphate kinases: is the Kornberg complex ubiquitous?
Trends Biochem. Sci.
33
577-582
2008
Ostreococcus tauri (A0A090M3D0), Methanocorpusculum labreanum (A2SQZ9), Neopyropia yezoensis (A2VBB6), Ostreococcus sp. 'lucimarinus' (A4RQI1), Escherichia coli (P0A7B1), Physcomitrium patens (Q2MEV6), Dictyostelium discoideum (Q54BM7), Dictyostelium discoideum
Shimane, M.; Sugai, Y.; Kainuma, R.; Natsume, M.; Kawaide, H.
Mevalonate-dependent enzymatic synthesis of amorphadiene driven by an ATP-regeneration system using polyphosphate kinase
Biosci. Biotechnol. Biochem.
76
1558-1560
2012
Escherichia coli
Lu, Y.; Zhang, C.; Lai, Q.; Zhao, H.; Xing, X.H.
Improved hydrogen production under microaerophilic conditions by overexpression of polyphosphate kinase in Enterobacter aerogenes
Enzyme Microb. Technol.
48
187-192
2011
Escherichia coli
Peng, L.; Luo, W.Y.; Zhao, T.; Wan, C.S.; Jiang, Y.; Chi, F.; Zhao, W.; Cao, H.; Huang, S.H.
Polyphosphate kinase 1 is required for the pathogenesis process of meningitic Escherichia coli K1 (RS218)
Future Microbiol.
7
411-423
2012
Escherichia coli, Escherichia coli K1 (RS218)
Lu, Y.; Lai, Q.; Zhang, C.; Zhao, H.; Xing, X.
Alteration of energy metabolism in Enterobacter aerogenes by external addition of pyrophosphates and overexpression of polyphosphate kinase for enhanced hydrogen production
J. Chem. Technol. Biotechnol.
87
996-1003
2012
Escherichia coli
-
Chen, J.; Su, L.; Wang, X.; Zhang, T.; Liu, F.; Chen, H.; Tan, C.
Polyphosphate kinase mediates antibiotic tolerance in extraintestinal pathogenic Escherichia coli PCN033
Front. Microbiol.
7
724
2016
Escherichia coli, Escherichia coli PCN033
Liang, M.; Frank, S.; Luensdorf, H.; Warren, M.J.; Prentice, M.B.
Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli
Biotechnol. J.
12
1600415
2017
Escherichia coli
Burda-Grabowska, M.; Macegoniuk, K.; Flick, R.; Nocek, B.; Joachimiak, A.; Yakunin, A.; Mucha, A.; Berlicki, A.
Bisphosphonic acids and related compounds as inhibitors of nucleotide- and polyphosphate-processing enzymes A PPK1 and PPK2 case study
Chem. Biol. Drug Des.
93
1197-1206
2019
Cytophaga hutchinsonii (A0A6N4SMB5), Escherichia coli (P0A7B1), Cytophaga hutchinsonii DSM 1761 (A0A6N4SMB5)
Gautam, L.K.; Sharma, P.; Capalash, N.
Bacterial polyphosphate kinases revisited role in pathogenesis and therapeutic potential
Curr. Drug Targets
20
292-301
2019
Bacillus cereus, Porphyromonas gingivalis, Escherichia coli, Francisella tularensis, Helicobacter pylori, Neisseria meningitidis, Proteus mirabilis, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli K1 (RS218)
Rudat, A.K.; Pokhrel, A.; Green, T.J.; Gray, M.J.
Mutations in Escherichia coli polyphosphate kinase that lead to dramatically increased in vivo polyphosphate levels
J. Bacteriol.
200
e00697-17
2018
Escherichia coli (P0A7B1), Escherichia coli, Escherichia coli K12 (P0A7B1)
Bashatwah, R.M.; Khanfar, M.A.; Bardaweel, S.K.
Discovery of potent polyphosphate kinase 1 (PPK1) inhibitors using structure-based exploration of PPK1Pharmacophoric space coupled with docking analyses
J. Mol. Recognit.
31
e2726
2018
Escherichia coli (P0A7B1), Escherichia coli, Escherichia coli K12 (P0A7B1)
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