BRENDA - Enzyme Database
show all sequences of 2.7.4.B2

Polyphosphate:AMP phosphotransferase and polyphosphate:ADP phosphotransferase activities of Pseudomonas aeruginosa

Ishige, K.; Noguchi, T.; Biochem. Biophys. Res. Commun. 281, 821-826 (2001)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Pseudomonas aeruginosa
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
AMP + [phosphate]n
Pseudomonas aeruginosa
best substrate
ADP + [phosphate]n-1
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
-
-
-
Purification (Commentary)
Commentary
Organism
by gel filtration, separation from polyphosphate kinase activity
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
AMP + (phosphate)n
the activity originates from combined action of the polyphosphate:ADP phosphotransferase and adenylate kinase
718728
Pseudomonas aeruginosa
ADP + (phosphate)n-1
-
-
-
?
AMP + [phosphate]n
best substrate
718728
Pseudomonas aeruginosa
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
best substrate is [phosphate]15
718728
Pseudomonas aeruginosa
ADP + [phosphate]n-1
-
-
-
?
additional information
the partially purified polyphosphate:ADP phosphotransferase is independent of polyphosphate kinase, PPK, and can function as polyphosphate-dependent nucleoside diphosphate kinase, PADP, which most prefers GDP to the other three nucleoside diphosphates as a phospho-acceptor. Both of the polyphosphate-utilizing activities require short polyphosphate as a phospho-donor whose chain length is below 75. The PAP activity mainly originates from the combined action of adenylate kinase, ADK, and the PADP independent of PPK. Each partially purified enzyme alone cannot mediate phosphorylation of AMP with polyphosphate, but coincubation of the both enzymes results in a marked expression of PAP activity, confirming that PADP and ADK constitute the PAP
718728
Pseudomonas aeruginosa
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Pseudomonas aeruginosa
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Pseudomonas aeruginosa
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Pseudomonas aeruginosa
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
AMP + [phosphate]n
Pseudomonas aeruginosa
best substrate
ADP + [phosphate]n-1
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
by gel filtration, separation from polyphosphate kinase activity
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
AMP + (phosphate)n
the activity originates from combined action of the polyphosphate:ADP phosphotransferase and adenylate kinase
718728
Pseudomonas aeruginosa
ADP + (phosphate)n-1
-
-
-
?
AMP + [phosphate]n
best substrate
718728
Pseudomonas aeruginosa
ADP + [phosphate]n-1
-
-
-
?
AMP + [phosphate]n
best substrate is [phosphate]15
718728
Pseudomonas aeruginosa
ADP + [phosphate]n-1
-
-
-
?
additional information
the partially purified polyphosphate:ADP phosphotransferase is independent of polyphosphate kinase, PPK, and can function as polyphosphate-dependent nucleoside diphosphate kinase, PADP, which most prefers GDP to the other three nucleoside diphosphates as a phospho-acceptor. Both of the polyphosphate-utilizing activities require short polyphosphate as a phospho-donor whose chain length is below 75. The PAP activity mainly originates from the combined action of adenylate kinase, ADK, and the PADP independent of PPK. Each partially purified enzyme alone cannot mediate phosphorylation of AMP with polyphosphate, but coincubation of the both enzymes results in a marked expression of PAP activity, confirming that PADP and ADK constitute the PAP
718728
Pseudomonas aeruginosa
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Pseudomonas aeruginosa
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Pseudomonas aeruginosa
General Information
General Information
Commentary
Organism
additional information
overexpression in strain PAO1 leads to a massive production of polyphosphate kinase, PPK, and a marked enhancement of polyphosphate-synthesizing activity, while the PAP activity is not affected by overproduction of PPK
Pseudomonas aeruginosa
General Information (protein specific)
General Information
Commentary
Organism
additional information
overexpression in strain PAO1 leads to a massive production of polyphosphate kinase, PPK, and a marked enhancement of polyphosphate-synthesizing activity, while the PAP activity is not affected by overproduction of PPK
Pseudomonas aeruginosa
Other publictions for EC 2.7.4.B2
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)
737499
Motomura
A new subfamily of polyphospha ...
Meiothermus ruber, Meiothermus ruber NBRC 106122
Appl. Environ. Microbiol.
80
2602-2608
2014
1
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1
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2
-
-
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2
2
6
-
2
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1
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6
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11
1
1
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1
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1
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1
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2
2
6
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1
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6
-
11
1
1
1
1
-
1
-
-
-
-
3
3
-
-
-
738411
Jyoti Roy
-
Polyphosphate kinase from Leis ...
Leishmania donovani, Leishmania donovani MHOM/IN/83/AG83
Int. J. Drug Develop. Res.
6
159-164
2014
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-
-
-
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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
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3
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1
3
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5
-
1
-
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1
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1
1
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-
-
720887
Zhang
Inorganic polyphosphate in the ...
Myxococcus xanthus
Proc. Natl. Acad. Sci. USA
102
13416-13420
2005
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722513
Shiba
Polyphosphate:AMP phosphotrans ...
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
J. Bacteriol.
187
1859-1865
2005
-
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1
-
-
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1
3
-
2
1
2
-
6
-
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1
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-
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3
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16
1
1
1
1
3
1
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1
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1
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1
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3
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2
1
2
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-
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1
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3
-
16
1
1
1
1
3
1
-
1
-
-
1
1
-
3
3
720949
Shi
Inorganic polyphosphate in Bac ...
Bacillus cereus
Proc. Natl. Acad. Sci. USA
49
17061-17065
2004
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-
-
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1
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6
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722511
Itoh
Polyphosphate synthetic activi ...
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
J. Bacteriol.
186
5178-5181
2004
-
-
-
-
-
-
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2
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1
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7
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5
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14
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1
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1
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2
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1
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7
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14
-
1
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-
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1
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-
-
-
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-
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-
645130
Kameda
A novel ATP regeneration syste ...
Acinetobacter johnsonii, Myxococcus xanthus, Myxococcus xanthus DK101
J. Biosci. Bioeng.
91
557-563
2001
-
2
-
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2
2
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3
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3
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1
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1
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8
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2
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2
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2
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2
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1
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1
1
8
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2
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2
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718728
Ishige
Polyphosphate:AMP phosphotrans ...
Pseudomonas aeruginosa
Biochem. Biophys. Res. Commun.
281
821-826
2001
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1
1
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4
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4
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1
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1
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1
1
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718766
Tanaka
-
A sensitive method for detecti ...
Acinetobacter johnsonii
Biochem. Eng. J.
9
193-197
2001
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4
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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
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1
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1
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4
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1
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1
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1
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2
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2
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1
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1
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718620
Resnick
In vitro ATP regeneration from ...
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
Appl. Environ. Microbiol.
66
2045-2051
2000
-
1
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-
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-
-
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1
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2
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6
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11
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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
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11
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1
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1
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-
-
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2
2
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718947
Shiba
-
Inorganic polyphosphate and po ...
Escherichia coli
Biochemistry
65
375-384
2000
-
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1
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1
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720883
Ishige
Inorganic polyphosphate kinase ...
Escherichia coli, Escherichia coli JM109
Proc. Natl. Acad. Sci. USA
97
14168-14171
2000
-
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4
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34
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4
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1
1
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721769
Bonting
Purification and properties of ...
Acinetobacter johnsonii, Acinetobacter johnsonii 210A
Biodegradation
10
393-398
1999
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3
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1
1
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722288
Bark
Polyphosphate-dependent enzyme ...
Cellulosimicrobium cellulans, no activity in Aureobacterium saperdae, no activity in Curtobacterium sp., no activity in Shewanella putrefaciens
FEMS Microbiol. Lett.
107
133-138
1993
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719681
Bonting
Properties of polyphosphate:AM ...
Acinetobacter johnsonii, Acinetobacter johnsonii 210A, Acinetobacter sp., Acinetobacter sp. 210A
J. Bacteriol.
173
6484-6488
1991
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8
4
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2
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2
1
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6
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2
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718617
van Groenstijn
Polyphosphate-degrading enzyme ...
Acinetobacter sp.
Appl. Environ. Microbiol.
55
219-223
1989
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