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Information on EC 3.6.1.11 - exopolyphosphatase and Organism(s) Escherichia coli and UniProt Accession P0A840
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3.6.1.11 exopolyphosphataseSpecify your search results
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
exopolyphosphatase, polyphosphate phosphatase, polyphosphate phosphohydrolase, exopolypase, rv0496, exopoly(p)ase, pappx, exopolyphosphatase 1, lmppx, high molecular weight exopolyphosphatase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid phosphoanhydride phosphohydrolase
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exopoly(P)ase
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ExopolyPase
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Gra-Pase
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metaphosphatase
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phosphatase, exopoly-
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PPX
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate
the interaction of the enzyme with polyphosphate is independent on cation concentration, binding is not driven by entropy from release of polyelectrolyte condensed cations
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
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SYSTEMATIC NAME
IUBMB Comments
polyphosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
9024-85-5
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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
additional information
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contains an exopolyphosphatase, EC 3.6.1.11 and a guanosine pentaphosphate phosphohydrolase with long-chain exopolyphosphatase activity, EC 3.6.1.40
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additional information
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exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage
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additional information
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exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage
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additional information
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substrates are commercial sodium phosphate glass with 25-PP25-, 65-PP65-, or PPK-synthesized polyphosphate with 700-PP700-average number of residues. Released phosphate is detected by the malachite green method at 630 nm
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additional information
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substrates are commercial sodium phosphate glass with 25-PP25-, 65-PP65-, or PPK-synthesized polyphosphate with 700-PP700-average number of residues. Released phosphate is detected by the malachite green method at 630 nm
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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
additional information
?
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exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage
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additional information
?
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exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
KD: 46.9 +/- 5.66 micorM Co2+ with p-nitrophenyl phosphate, KD: 10.7 +/- 1.07 microM Co2+ with 5'-AMP
Mg2+
KD: 224.7 +/- 35.1 microM Mg2+ with p-nitrophenyl phosphate, KD: 140.0 +/- 9.99 microM Mg2+ with 5'-AMP
Mn2+
KD: 7.24 +/- 0.71 microM Mn2+ with p-nitrophenyl phosphate, KD: 2.23 +/- 0.14 micorM Mn2+ with 5'-AMP
Ni2+
KD: 72.3 +/- 7.61 microM Ni2+ with p-nitrophenyl phosphate, KD: 29.4 +/- 3.69 microM Ni2+ with 5'-AMP
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Polyphosphate
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polyP15, 50% inhibition at 200fold polymer molar excess over the long-chain polyphosphate substrate
Tetrapolyphosphate
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50% inhibition at 2000fold polymer molar excess over the long-chain polyP substrate
tripolyphosphate
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weak inhibition at 2000fold polymer molar excess over the long-chain polyP substrate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the exopolyphosphatase belongs to the ASKHA protein superfamily
malfunction
analysis of single ppx- or ppk- mutants and of the double mutant, demonstrate a relationship between these genes and the survival capacity
physiological function
the exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Polyphosphate plays a remarkable role in pathogenesis, survival and stress tolerance
additional information
additional information
substrate binding structure analysis, different computational approaches, site-direct mutagenesis and kinetic data are applied to understand the relationship between structure and function of exopolyphosphatase. Enzyme residue H378 is proposed as a fundamental gatekeeper for the recognition of long chain polyphosphate. Implication of H378 protonation state, overview. Electrostatic and energy calculations and molecular docking study, molecular dynamics simulations, overview. The frontal surface of the protein has a clear predominance of electropositive potential and the minimum binding energies are also obtained in that surface. This is favored by interaction with R166,K197, H382, G380, and K414. Other favorable region is formed by residues K353, K428, K429, K430 and Q431 in the joint of domains I and IV. On the contrary, the binding energies of the back side of the protein surface are unfavorable to bind polyphosphate, consistent with a predominance of electronegative potential. Indeed, ecPpx is characterized by a clear division between electropositive (frontal) and electronegative (back) potential
additional information
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substrate binding structure analysis, different computational approaches, site-direct mutagenesis and kinetic data are applied to understand the relationship between structure and function of exopolyphosphatase. Enzyme residue H378 is proposed as a fundamental gatekeeper for the recognition of long chain polyphosphate. Implication of H378 protonation state, overview. Electrostatic and energy calculations and molecular docking study, molecular dynamics simulations, overview. The frontal surface of the protein has a clear predominance of electropositive potential and the minimum binding energies are also obtained in that surface. This is favored by interaction with R166,K197, H382, G380, and K414. Other favorable region is formed by residues K353, K428, K429, K430 and Q431 in the joint of domains I and IV. On the contrary, the binding energies of the back side of the protein surface are unfavorable to bind polyphosphate, consistent with a predominance of electronegative potential. Indeed, ecPpx is characterized by a clear division between electropositive (frontal) and electronegative (back) potential
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 5% glycerol, 0.5 M NaCl, pH 7.5, no loss in activity after several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ppx, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strains XL10-Gold and BL21-CodonPlus
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Akiyama, M.; Crooke, E.; Kornberg, A.
An exopolyphosphatase of Escherichia coli. The enzyme and its ppx gene in a polyphosphate operon
J. Biol. Chem.
268
633-639
1993
Escherichia coli
Keasling, J.D.; Bertsch, L.; Kornberg, A.
Guanosine pentaphosphate phosphohydrolase of Escherichia coli is a long-chain exopolyphosphatase
Proc. Natl. Acad. Sci. USA
90
7029-7033
1993
Escherichia coli
Bolesch, D.G.; Keasling, J.D.
The effect of monovalent ions on polyphosphate binding to Escherichia coli exopolyphosphatase
Biochem. Biophys. Res. Commun.
274
236-241
2000
Escherichia coli
Proudfoot, M.; Kuznetsova, E.; Brown, G.; Rao, N.N.; Kitagawa, M.; Mori, H.; Savchenko, A.; Yakunin, A.F.
General Enzymatic Screens Identify Three New Nucleotidases in Escherichia coli. Biochemical Characterization of SurE, YfbR, and Yjjg
J. Biol. Chem.
279
54687-54694
2004
Escherichia coli (P0A840)
Rangarajan, E.S.; Nadeau, G.; Li, Y.; Wagner, J.; Hung, M.N.; Schrag, J.D.; Cygler, M.; Matte, A.
The structure of the exopolyphosphatase (PPX) from Escherichia coli O157:H7 suggests a binding mode for long polyphosphate chains
J. Mol. Biol.
359
1249-1260
2006
Escherichia coli
Alvarado, J.; Ghosh, A.; Janovitz, T.; Jauregui, A.; Hasson, M.S.; Sanders, D.A.
Origin of exopolyphosphatase processivity: Fusion of an ASKHA phosphotransferase and a cyclic nucleotide phosphodiesterase homolog
Structure
14
1263-1272
2006
Escherichia coli
Boetsch, C.; Aguayo-Villegas, D.R.; Gonzalez-Nilo, F.D.; Lisa, A.T.; Beassoni, P.R.
Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
Arch. Biochem. Biophys.
606
64-72
2016
Escherichia coli (P0AFL6), Escherichia coli
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