BRENDA - Enzyme Database show
show all sequences of 3.6.1.11

Exopolyphosphatases PPX1 and PPX2 from Corynebacterium glutamicum[down-pointing small open triangle]

Lindner, S.N.; Knebel, S:; Wesseling,H.; Schoberth, S.M.; Wendisch, V.F.; Appl. Environ. Microbiol. 75, 3161-3170 (2009)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
CaCl2, BaCl2, CuSO4, and SnCl2 do not show any activating effect on PPX2
Corynebacterium glutamicum
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli, overexpression of ppx2 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain; overexpression of ppx1 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain
Corynebacterium glutamicum
Inhibitors
Inhibitors
Commentary
Organism
Structure
ADP
-
Corynebacterium glutamicum
ATP
-
Corynebacterium glutamicum
Ca2+
PPX2 is inhibited by millimolar concentrations
Corynebacterium glutamicum
CaCl2
3.8 mM CaCl2 leads to half-maximal inhibition of His-tagged PPX2
Corynebacterium glutamicum
dATP
-
Corynebacterium glutamicum
dGTP
-
Corynebacterium glutamicum
GTP
-
Corynebacterium glutamicum
ITP
-
Corynebacterium glutamicum
Mg2+
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 10 mM MnCl2
Corynebacterium glutamicum
Mn2+
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 3.5 mM MnCl2
Corynebacterium glutamicum
Pyrophosphate
8.2 mM pyrophosphate leads to half-maximal inhibition of His-tagged PPX2
Corynebacterium glutamicum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
Triphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
0.11
-
Tetraphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
enzyme is stimulated 0.26fold at a concentration of 2 mM
Corynebacterium glutamicum
K+
PPX2 activity is increased, 25 mM KCl resulting in a 3fold increase in the specific activity
Corynebacterium glutamicum
Mg2+
enzyme requires Mg2+ cations but is inhibited by higher concentrations, Mg2+ shows the highest stimulation at 2 mM
Corynebacterium glutamicum
Mn2+
enzyme is stimulated 0.86fold at a concentration of 2 mM
Corynebacterium glutamicum
Zn2+
enzyme is stimulated 0.11fold at a concentration of 2 mM
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(phosphate)n + H2O
Corynebacterium glutamicum
degradation of polyphosphate
(phosphate)n-1 + phosphate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium glutamicum
Q8NRR8
-
-
Corynebacterium glutamicum
Q8NT99
-
-
Purification (Commentary)
Commentary
Organism
recombinant ppx2 enzyme is purified by Ni-nitrilotriacetic acid chromatography
Corynebacterium glutamicum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
when various short- to medium-chain PolyPs are tested, His-tagged PPX2 is most active with polyphosphates of 3-20 phosphate residues
Corynebacterium glutamicum
0.04
-
analysis of the constructed deletion mutant ppx2 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
Corynebacterium glutamicum
0.08
-
analysis of the constructed deletion mutant ppx1 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
Corynebacterium glutamicum
0.12
-
wild type, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2; wild type, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
Corynebacterium glutamicum
0.43
-
overexpression of ppx1 increase the specific activity of exopolyphosphatase by 4fold compared to that of the empty vector control
Corynebacterium glutamicum
0.8
-
crude cell extracts of wild type strain pVWEx1-ppx2 show 6fold higher exopolyphosphatase activity than those of wild type pVWEx1
Corynebacterium glutamicum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(phosphate)n + H2O
degradation of polyphosphate
701387
Corynebacterium glutamicum
(phosphate)n-1 + phosphate
-
-
-
?
additional information
PPX2 is active with short-chain polyphosphates, even accepting diphosphate
701387
Corynebacterium glutamicum
?
-
-
-
-
tetraphosphate + H2O
-
701387
Corynebacterium glutamicum
triphosphate + phosphate
-
-
-
?
triphosphate + H2O
-
701387
Corynebacterium glutamicum
diphosphate + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
determined by gel filtration
Corynebacterium glutamicum
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
-
Corynebacterium glutamicum
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
25
40
at pH 6.8, 2 mM MgCl2 and 25 mM KCl, no significant loss of activity is observed after 60 min
Corynebacterium glutamicum
45
-
after preheating at 45C for 30 and 60 min, 70% and 40% of the PPX2 activity remains
Corynebacterium glutamicum
50
-
after preheating at 50C, His-tagged PPX2 loses its activity quickly, after incubation for 60 min, no activity remains
Corynebacterium glutamicum
60
-
complete inactivation of His-tagged PPX2 within 5 min
Corynebacterium glutamicum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
Triphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
0.9
-
Tetraphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
highest activity of recombinant His-tagged PPX2 is reached in 50 mM PIPES buffer
Corynebacterium glutamicum
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
dGTP
-
Corynebacterium glutamicum
0.6
-
ADP
-
Corynebacterium glutamicum
0.6
-
dATP
-
Corynebacterium glutamicum
0.8
-
GTP
-
Corynebacterium glutamicum
0.8
-
ITP
-
Corynebacterium glutamicum
2.6
-
ATP
-
Corynebacterium glutamicum
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
CaCl2, BaCl2, CuSO4, and SnCl2 do not show any activating effect on PPX2
Corynebacterium glutamicum
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression of ppx1 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain
Corynebacterium glutamicum
expression in Escherichia coli, overexpression of ppx2 gene in Corynebacterium glutamicum results in higher exopolyphosphatase activities in crude extracts and deletion of the gene with lower activities than those of the wild-type strain
Corynebacterium glutamicum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ADP
-
Corynebacterium glutamicum
ATP
-
Corynebacterium glutamicum
Ca2+
PPX2 is inhibited by millimolar concentrations
Corynebacterium glutamicum
CaCl2
3.8 mM CaCl2 leads to half-maximal inhibition of His-tagged PPX2
Corynebacterium glutamicum
dATP
-
Corynebacterium glutamicum
dGTP
-
Corynebacterium glutamicum
GTP
-
Corynebacterium glutamicum
ITP
-
Corynebacterium glutamicum
Mg2+
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 10 mM MnCl2
Corynebacterium glutamicum
Mn2+
PPX2 is inhibited by millimolar concentrations, activity is reduced 2fold at 3.5 mM MnCl2
Corynebacterium glutamicum
Pyrophosphate
8.2 mM pyrophosphate leads to half-maximal inhibition of His-tagged PPX2
Corynebacterium glutamicum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.4
-
dGTP
-
Corynebacterium glutamicum
0.6
-
ADP
-
Corynebacterium glutamicum
0.6
-
dATP
-
Corynebacterium glutamicum
0.8
-
GTP
-
Corynebacterium glutamicum
0.8
-
ITP
-
Corynebacterium glutamicum
2.6
-
ATP
-
Corynebacterium glutamicum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
Triphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
0.11
-
Tetraphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
enzyme is stimulated 0.26fold at a concentration of 2 mM
Corynebacterium glutamicum
K+
PPX2 activity is increased, 25 mM KCl resulting in a 3fold increase in the specific activity
Corynebacterium glutamicum
Mg2+
enzyme requires Mg2+ cations but is inhibited by higher concentrations, Mg2+ shows the highest stimulation at 2 mM
Corynebacterium glutamicum
Mn2+
enzyme is stimulated 0.86fold at a concentration of 2 mM
Corynebacterium glutamicum
Zn2+
enzyme is stimulated 0.11fold at a concentration of 2 mM
Corynebacterium glutamicum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(phosphate)n + H2O
Corynebacterium glutamicum
degradation of polyphosphate
(phosphate)n-1 + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant ppx2 enzyme is purified by Ni-nitrilotriacetic acid chromatography
Corynebacterium glutamicum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
when various short- to medium-chain PolyPs are tested, His-tagged PPX2 is most active with polyphosphates of 3-20 phosphate residues
Corynebacterium glutamicum
0.04
-
analysis of the constructed deletion mutant ppx2 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
Corynebacterium glutamicum
0.08
-
analysis of the constructed deletion mutant ppx1 reveal reduced exopolyphosphatase activity, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
Corynebacterium glutamicum
0.12
-
wild type, samples containing 50 mM PIPES, pH 6.8, 25 mM KCl, and 2 mM MgCl2
Corynebacterium glutamicum
0.43
-
overexpression of ppx1 increase the specific activity of exopolyphosphatase by 4fold compared to that of the empty vector control
Corynebacterium glutamicum
0.8
-
crude cell extracts of wild type strain pVWEx1-ppx2 show 6fold higher exopolyphosphatase activity than those of wild type pVWEx1
Corynebacterium glutamicum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(phosphate)n + H2O
degradation of polyphosphate
701387
Corynebacterium glutamicum
(phosphate)n-1 + phosphate
-
-
-
?
additional information
PPX2 is active with short-chain polyphosphates, even accepting diphosphate
701387
Corynebacterium glutamicum
?
-
-
-
-
tetraphosphate + H2O
-
701387
Corynebacterium glutamicum
triphosphate + phosphate
-
-
-
?
triphosphate + H2O
-
701387
Corynebacterium glutamicum
diphosphate + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
determined by gel filtration
Corynebacterium glutamicum
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
-
Corynebacterium glutamicum
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
25
40
at pH 6.8, 2 mM MgCl2 and 25 mM KCl, no significant loss of activity is observed after 60 min
Corynebacterium glutamicum
45
-
after preheating at 45C for 30 and 60 min, 70% and 40% of the PPX2 activity remains
Corynebacterium glutamicum
50
-
after preheating at 50C, His-tagged PPX2 loses its activity quickly, after incubation for 60 min, no activity remains
Corynebacterium glutamicum
60
-
complete inactivation of His-tagged PPX2 within 5 min
Corynebacterium glutamicum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.6
-
Triphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
0.9
-
Tetraphosphate
in 50 mM PIPES, pH 6.8 containing 25 mM KCl and 2 mM MgCl2
Corynebacterium glutamicum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
highest activity of recombinant His-tagged PPX2 is reached in 50 mM PIPES buffer
Corynebacterium glutamicum
Other publictions for EC 3.6.1.11
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734338
Andreeva
Purification and properties of ...
Saccharomyces cerevisiae
J. Biosci. Bioeng.
119
52-56
2015
1
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1
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1
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2
3
1
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2
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1
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6
1
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1
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6
1
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-
-
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1
1
-
-
-
735010
Andreeva
Polyphosphatase PPN1 of Saccha ...
Saccharomyces cerevisiae
PLoS ONE
10
e0119594
2015
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-
1
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-
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1
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1
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1
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4
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734644
Albi
Two exopolyphosphatases with d ...
Chlorobaculum tepidum, Chlorobaculum tepidum DSM 12025
Microbiology
160
2067-2078
2014
-
-
1
-
-
-
1
6
-
4
4
-
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6
-
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5
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18
2
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6
1
2
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6
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4
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5
-
18
2
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6
2
2
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6
6
734647
Gallarato
Exopolyphosphatase of Pseudomo ...
Pseudomonas aeruginosa
Microbiology
160
406-417
2014
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-
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2
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1
1
1
1
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735334
Malde
Functional characterization of ...
Campylobacter jejuni, Campylobacter jejuni 81-176
Virulence
5
521-533
2014
-
-
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-
-
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4
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1
2
-
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735058
Choi
The two PPX-GppA homologues fr ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
PLoS ONE
7
e42561
2012
-
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1
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2
3
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4
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5
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3
1
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1
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2
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3
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4
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8
-
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3
1
-
-
-
-
-
-
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3
3
711604
Luginbuehl
The exopolyphosphatase TbrPPX1 ...
Trypanosoma brucei, Trypanosoma brucei 427
BMC Microbiol.
11
4-4
2011
1
-
1
-
-
-
2
1
1
1
2
-
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4
-
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1
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6
-
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1
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1
1
1
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1
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1
2
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1
1
1
2
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1
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6
-
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1
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1
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1
1
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719614
Campos
A mitochondrial membrane exopo ...
Rhipicephalus microplus
Int. J. Mol. Sci.
12
3525-3535
2011
3
-
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-
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3
2
2
-
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2
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1
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1
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3
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2
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1
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1
1
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720842
Thayil
The role of the novel exopolyp ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551
PLoS ONE
6
e28076
2011
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1
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1
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4
1
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2
2
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702901
Varela
New structural and functional ...
Pseudomonas sp.
BMC Microbiol.
10
7-7
2010
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11
6
2
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5
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Inactivation of PPX1 and PPN1 ...
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2
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8
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9
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12
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8
1
12
9
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1
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1
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1
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9
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1
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1
15
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697460
Campos
Exopolyphosphatases in nuclear ...
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Comp. Biochem. Physiol. B
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2008
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1
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1
1
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4
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1
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1
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687085
Campos
A mitochondrial exopolyphospha ...
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Insect Biochem. Mol. Biol.
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2007
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1
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Overexpression of a Zn2+-sensi ...
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1
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6
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3
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4
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1
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2
1
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687678
Tammenkoski
Kinetic and mutational analyse ...
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1
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1
1
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1
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6
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6
2
1
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1
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2
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1
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1
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Ugochukwu
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1
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1
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1
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1
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2
1
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1
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667765
Andreeva
High Molecular Mass Exopolypho ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
Biochemistry (Moscow)
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2006
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2
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668027
Lichko
Inorganic polyphosphates and e ...
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Biosci. Rep.
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2006
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2
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669880
Rangarajan
The structure of the exopolyph ...
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2006
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1
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1
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1
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1
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670175
Kulakovskaya
-
The effect of inactivation of ...
Saccharomyces cerevisiae
Microbiology
75
25-28
2006
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670176
Lichko
-
Inactivation of the PPN1 gene ...
Saccharomyces cerevisiae
Microbiology
75
253-258
2006
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2
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1
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1
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670910
Alvarado
Origin of exopolyphosphatase p ...
Escherichia coli
Structure
14
1263-1272
2006
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1
4
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2
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1
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1
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1
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1
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685297
Lichko
Inorganic polyphosphates and e ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae CRY
Biochemistry (Moscow)
71
1171-1175
2006
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1
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2
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1
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1
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4
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2
2
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1
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2
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690206
Lichko
Inorganic polyphosphate and ex ...
Saccharomyces cerevisiae
Yeast
23
735-740
2006
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1
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2
1
1
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2
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1
1
1
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1
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1
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2
2
1
1
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1
1
1
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1
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725894
Remonsellez
Copper tolerance of the thermo ...
Sulfolobus metallicus, Sulfolobus metallicus DSM 6482
Microbiology
152
59-66
2006
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1
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2
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2
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667750
Kulakovskaya
Accumulation of polyphosphates ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
Biochemistry
70
980-985
2005
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2
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2
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6
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1
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2
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2
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1
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668674
Pestov
Effects of inactivation of the ...
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823-828
2005
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1
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8
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1
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1
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8
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1
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654784
Lichko
Partial purification and chara ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae CRX
Biochemistry
69
270-274
2004
2
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4
3
4
1
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1
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8
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9
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4
7
2
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1
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9
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654785
Andreeva
Purification and properties of ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae VKM Y-1173
Biochemistry
69
387-393
2004
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6
2
7
4
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6
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1
1
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5
5
10
1
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1
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1
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8
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6
2
7
4
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1
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5
5
10
1
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1
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654886
Lichko
Inactivation of endopolyphosph ...
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Biochim. Biophys. Acta
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2004
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1
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1
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1
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1
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1
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656266
Proudfoot
General Enzymatic Screens Iden ...
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1
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10
7
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7
1
7
2
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7
1
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1
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1
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1
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10
1
7
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4
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7
1
7
2
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1
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Kulakovskaya
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654839
Lichko
Effect of PPX1 inactivation on ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1599
102-105
2002
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1
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1
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1
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656105
Rodrigues
An acidocalcisomal exopolyphos ...
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1
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3
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1
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1
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1
3
1
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657203
Lichko
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1
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Cardona
The exopolyphosphatase gene fr ...
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Appl. Environ. Microbiol.
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660737
Zago
Cloning and characterization o ...
Pseudomonas aeruginosa, Pseudomonas aeruginosa 8830
Appl. Environ. Microbiol.
65
2065-2071
1999
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209845
Andreeva
Purification and properties of ...
Saccharomyces cerevisiae
FEBS Lett.
429
194-196
1998
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209852
Guranowski
Adenosine 5'-tetraphosphate ph ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1380
232-238
1998
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4
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1
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209849
Kulakovskaya
Adenosine-5'-tetraphosphate an ...
Saccharomyces cerevisiae
Biochemistry
62
1051-1052
1997
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209851
Lorenz
Purification and characterizat ...
Tethya aurantium
Biochim. Biophys. Acta
1245
17-28
1995
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209846
Lorenz
Purification and characterizat ...
Saccharomyces cerevisiae
J. Biol. Chem.
269
22198-22204
1994
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209847
Wurst
A soluble exopolyphosphatase o ...
Saccharomyces cerevisiae
J. Biol. Chem.
269
10996-11001
1994
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209844
Akiyama
An exopolyphosphatase of Esche ...
Escherichia coli
J. Biol. Chem.
268
633-639
1993
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1
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209848
Keasling
Guanosine pentaphosphate phosp ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
90
7029-7033
1993
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209778
Curdova
Properties of apyrase and inor ...
Kitasatospora aureofaciens
Folia Microbiol. (Praha)
27
159-166
1982
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209834
Capaccio
-
The enzymes of polyphosphate m ...
Funneliformis mosseae
New Phytol.
91
81-91
1982
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209843
Jungnickel
-
Regulative properties of surfa ...
Cyberlindnera jadinii
Abh. Akad. Wiss. DDR Abt. Math. Naturwiss. Techn. , 3N, Microb. Enzymprod.
421-426
1981
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209842
Piccinnni
-
Inorganic phosphatases and pho ...
Euglena gracilis
Comp. Biochem. Physiol. B
57
281-284
1977
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209840
Afansieva
Polyphosphate phosphohydrolase ...
Magnusiomyces magnusii
Biochim. Biophys. Acta
321
336-347
1973
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13
1
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6
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1
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209841
Jungnickel
-
Significance of repressible po ...
Cyberlindnera jadinii, Lemna gibba, Lemna minor, Lemna trisulca, Riccia fluitans, Solanum tuberosum, Wolffia arrhiza
React. Mech. Control Prop. Phosphotransferases, Int. Symp. Meeting, Akad. Verl. Berlin
87-91
1971
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