BRENDA - Enzyme Database
show all sequences of 3.11.1.2

Divergence of chemical function in the alkaline phosphatase superfamily: structure and mechanism of the P-C bond cleaving enzyme phosphonoacetate hydrolase

Kim, A.; Benning, M.M.; OkLee, S.; Quinn, J.; Martin, B.M.; Holden, H.M.; Dunaway-Mariano, D.; Biochemistry 50, 3481-3494 (2011)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Phosphonoacetate
substrate activation, mechanism, overview
Pseudomonas fluorescens
Cloned(Commentary)
Cloned (Commentary)
Organism
recombinant expression in Escherichia coli strain JM105
Pseudomonas fluorescens
Crystallization (Commentary)
Crystallization (Commentary)
Organism
purified recombinant enzyme in in the presence of Zn2+, Mg2+, phosphonoformate and tartrate, from 30 mM K+BICINE, pH 8.5, and 1 mM ZnCl2, mixed with 10% poly(ethylene glycol) 8000, 100 mM Mg-acetate, and 5 mM phosphonoformate buffered at pH 7.0 with 100 mM MOPSO, X-ray diffraction structure determination and analysis at 2.8 A resolution, multiple isomorphous replacement with two heavy-atom derivatives
Pseudomonas fluorescens
Inhibitors
Inhibitors
Commentary
Organism
Structure
Phosphonoformate
competitive inhibitor, the phosphonoformate ligand and two zinc ions are bound at the core domain
Pseudomonas fluorescens
phosphonoproprionate
competitive inhibitor
Pseudomonas fluorescens
Phosphonopyruvate
competitive inhibitor
Pseudomonas fluorescens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
activates 2fold at 3 mM
Pseudomonas fluorescens
additional information
no effects by Mg2+, Ca2+, Ni2+, Mn2+, Cr2+, Cu2+ at 3 mM
Pseudomonas fluorescens
Zn2+
activates 10fold at 3 mM, the phosphonoformate ligand and two zinc ions are bound at the core domain
Pseudomonas fluorescens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44239
-
2 * 44239, sequence calculation and gel filtration
Pseudomonas fluorescens
93000
-
gel filtration, recombinant enzyme
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
Phosphonoacetate + H2O
Pseudomonas fluorescens
-
acetate + phosphate
-
-
?
Phosphonoacetate + H2O
Pseudomonas fluorescens 23F
-
acetate + phosphate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas fluorescens
-
-
-
Pseudomonas fluorescens 23F
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant enzyme from Escherichia coli strain JM105 by ammonium sulfate fractionation, and anion exchange, hydrophobic interaction, and hydroxylapatite chromatography, followed by gel filtration
Pseudomonas fluorescens
Reaction
Reaction
Commentary
Organism
Reaction ID
Phosphonoacetate + H2O = acetate + phosphate
structure and mechanism of the P-C bond cleaving enzyme, nucleophilic catalysis involving a zinc ion, overview. Modeling of the catalytic mechanism
Pseudomonas fluorescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
additional information
substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate
718897
Pseudomonas fluorescens
?
-
-
-
-
additional information
substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate
718897
Pseudomonas fluorescens 23F
?
-
-
-
-
Phosphonoacetate + H2O
-
718897
Pseudomonas fluorescens
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
-
718897
Pseudomonas fluorescens 23F
acetate + phosphate
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 44239, sequence calculation and gel filtration
Pseudomonas fluorescens
More
PAc hydrolase monomer is comprised of a large alpha/beta/alpha core domain of residues 1-245 and 367-388, 6-stranded mixed beta-sheet, and a smaller alpha/beta cap domain comprising residues 255-360, as 4-stranded antiparallel beta-sheet
Pseudomonas fluorescens
Synonyms
Synonyms
Commentary
Organism
PAc hydrolase
-
Pseudomonas fluorescens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
30
assay at
Pseudomonas fluorescens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
assay at
Pseudomonas fluorescens
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.049
-
Phosphonoformate
pH 7.0, 25°C
Pseudomonas fluorescens
0.19
-
Phosphonoformate
pH 7.0, 30°C
Pseudomonas fluorescens
1.2
-
phosphonoproprionate
pH 7.0, 30°C
Pseudomonas fluorescens
1.2
-
Phosphonopyruvate
pH 7.0, 30°C
Pseudomonas fluorescens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Phosphonoacetate
substrate activation, mechanism, overview
Pseudomonas fluorescens
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression in Escherichia coli strain JM105
Pseudomonas fluorescens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant enzyme in in the presence of Zn2+, Mg2+, phosphonoformate and tartrate, from 30 mM K+BICINE, pH 8.5, and 1 mM ZnCl2, mixed with 10% poly(ethylene glycol) 8000, 100 mM Mg-acetate, and 5 mM phosphonoformate buffered at pH 7.0 with 100 mM MOPSO, X-ray diffraction structure determination and analysis at 2.8 A resolution, multiple isomorphous replacement with two heavy-atom derivatives
Pseudomonas fluorescens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Phosphonoformate
competitive inhibitor, the phosphonoformate ligand and two zinc ions are bound at the core domain
Pseudomonas fluorescens
phosphonoproprionate
competitive inhibitor
Pseudomonas fluorescens
Phosphonopyruvate
competitive inhibitor
Pseudomonas fluorescens
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.049
-
Phosphonoformate
pH 7.0, 25°C
Pseudomonas fluorescens
0.19
-
Phosphonoformate
pH 7.0, 30°C
Pseudomonas fluorescens
1.2
-
phosphonoproprionate
pH 7.0, 30°C
Pseudomonas fluorescens
1.2
-
Phosphonopyruvate
pH 7.0, 30°C
Pseudomonas fluorescens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
activates 2fold at 3 mM
Pseudomonas fluorescens
additional information
no effects by Mg2+, Ca2+, Ni2+, Mn2+, Cr2+, Cu2+ at 3 mM
Pseudomonas fluorescens
Zn2+
activates 10fold at 3 mM, the phosphonoformate ligand and two zinc ions are bound at the core domain
Pseudomonas fluorescens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44239
-
2 * 44239, sequence calculation and gel filtration
Pseudomonas fluorescens
93000
-
gel filtration, recombinant enzyme
Pseudomonas fluorescens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
Phosphonoacetate + H2O
Pseudomonas fluorescens
-
acetate + phosphate
-
-
?
Phosphonoacetate + H2O
Pseudomonas fluorescens 23F
-
acetate + phosphate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain JM105 by ammonium sulfate fractionation, and anion exchange, hydrophobic interaction, and hydroxylapatite chromatography, followed by gel filtration
Pseudomonas fluorescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
additional information
substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate
718897
Pseudomonas fluorescens
?
-
-
-
-
additional information
substrate specificity, overview. No activity with fosfomycin or phosphonopyruvate
718897
Pseudomonas fluorescens 23F
?
-
-
-
-
Phosphonoacetate + H2O
-
718897
Pseudomonas fluorescens
acetate + phosphate
-
-
-
?
Phosphonoacetate + H2O
-
718897
Pseudomonas fluorescens 23F
acetate + phosphate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 44239, sequence calculation and gel filtration
Pseudomonas fluorescens
More
PAc hydrolase monomer is comprised of a large alpha/beta/alpha core domain of residues 1-245 and 367-388, 6-stranded mixed beta-sheet, and a smaller alpha/beta cap domain comprising residues 255-360, as 4-stranded antiparallel beta-sheet
Pseudomonas fluorescens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
30
assay at
Pseudomonas fluorescens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
assay at
Pseudomonas fluorescens
General Information
General Information
Commentary
Organism
evolution
the P-C bond cleaving enzyme phosphonoacetate hydrolase belongs to the alkaline phosphatase superfamily
Pseudomonas fluorescens
metabolism
the enzyme is involved in the 2-aminoethylphosphonic acid degradation pathway, overview
Pseudomonas fluorescens
General Information (protein specific)
General Information
Commentary
Organism
evolution
the P-C bond cleaving enzyme phosphonoacetate hydrolase belongs to the alkaline phosphatase superfamily
Pseudomonas fluorescens
metabolism
the enzyme is involved in the 2-aminoethylphosphonic acid degradation pathway, overview
Pseudomonas fluorescens
Other publictions for EC 3.11.1.2
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
Synonyms
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)
734593
Perry
A microfluidic approach for pr ...
Sinorhizobium meliloti
Lab Chip
13
3183-3187
2013
-
-
-
1
-
-
-
-
-
-
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-
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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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-
-
-
-
-
-
-
-
-
-
-
-
733908
Villarreal-Chiu
The genes and enzymes of phosp ...
Pseudomonas fluorescens
Front. Microbiol.
3
19
2012
-
-
1
-
-
-
-
-
-
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1
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2
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1
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2
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1
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1
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2
-
-
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-
-
-
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2
2
-
-
-
718897
Kim
Divergence of chemical functio ...
Pseudomonas fluorescens, Pseudomonas fluorescens 23F
Biochemistry
50
3481-3494
2011
1
-
1
1
-
-
3
-
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3
2
2
-
6
-
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1
1
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4
2
1
1
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1
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3
4
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1
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4
2
1
-
-
-
1
-
-
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2
2
-
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-
719273
Agarwal
Structural and mechanistic ins ...
Sinorhizobium meliloti
Chem. Biol.
18
1230-1240
2011
-
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1
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1
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1
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3
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1
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2
2
-
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-
719938
Borisova
Genetic and biochemical charac ...
Sinorhizobium meliloti
J. Biol. Chem.
286
22283-22290
2011
-
-
1
-
1
-
-
2
-
1
1
1
-
4
-
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1
-
-
-
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1
1
1
1
-
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2
1
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1
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1
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2
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1
1
1
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1
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-
1
1
1
-
-
2
1
-
-
-
-
1
1
-
1
1
720399
Cooley
Phosphonoacetate biosynthesis: ...
Roseovarius nubinhibens
Microbiology
80
335-340
2011
-
-
-
-
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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
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-
-
-
-
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1
1
-
-
-
697646
Gilbert
Potential for phosphonoacetate ...
Burkholderia ambifaria, Burkholderia ambifaria AMMD, Burkholderia multivorans, Candidatus Solibacter usitatus, Candidatus Solibacter usitatus Ellin6076, Cupriavidus necator, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1, Emiliania huxleyi, Karenia mikimotoi, no activity in Vibrio shiloi, Paraburkholderia xenovorans, Photobacterium rosenbergii, Photobacterium rosenbergii CC006, Rhodopseudomonas palustris, Rhodopseudomonas palustris CGA009, Sinorhizobium medicae, Sinorhizobium medicae WSM419, Sinorhizobium meliloti, Sorangium cellulosum, Verminephrobacter eiseniae, Verminephrobacter eiseniae EF01-2, Vibrio campbellii, Vibrio campbellii CC028, Vibrio harveyi
Environ. Microbiol.
11
111-125
2009
-
-
15
-
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-
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28
-
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17
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670346
Forlani
Phosphonoacetic acid utilizati ...
Penicillium oxalicum
Mycol. Res.
110
1455-1463
2006
-
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3
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683482
O'Loughlin
A role for carbon catabolite r ...
Agromyces fucosus, Agromyces fucosus Vs2
FEMS Microbiol. Lett.
261
133-140
2006
-
-
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4
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684053
Klimek-Ochab
Phosphonoacetate hydrolase fro ...
Penicillium oxalicum
Res. Microbiol.
157
125-135
2006
-
-
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1
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2
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3
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1
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1
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1
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1
1
1
1
1
-
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-
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-
-
655816
McGrath
-
A comparison of three bacteria ...
Curtobacterium sp., Curtobacterium sp. PA1, Pseudomonas sp., Pseudomonas sp. PA2
J. Appl. Microbiol.
86
834-840
1999
-
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18
2
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8
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4
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4
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8
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2
2
2
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2
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18
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2
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8
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4
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2
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8
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2
2
2
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2
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22933
Kulakova
Cloning of the phosphonoacetat ...
Pseudomonas fluorescens
Gene
195
49-53
1997
-
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1
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1
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4
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22930
McGrath
The purification and propertie ...
Pseudomonas fluorescens 23F, Pseudomonas fluorescens
Eur. J. Biochem.
234
225-230
1995
-
1
-
-
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5
1
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3
2
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5
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1
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1
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1
2
1
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1
1
1
1
1
1
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1
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5
-
1
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3
2
-
-
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1
-
1
-
1
2
1
1
1
1
1
1
1
-
-
-
-
-
-
-
-
22931
McGrath
-
A plate assay for the detectio ...
Pseudomonas fluorescens, Pseudomonas fluorescens 23F
Biotechnol. Tech.
9
497-502
1995
-
-
-
-
-
-
-
-
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4
-
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2
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-
-
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-
22932
McMullan
In vitro characterization of a ...
Pseudomonas fluorescens
J. Bacteriol.
176
320-324
1994
-
-
-
-
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-
6
-
-
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1
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3
-
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2
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6
-
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1
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2
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