BRENDA - Enzyme Database
show all sequences of 3.1.3.75

Using a molecular model and kinetic experiments in the presence of divalent cations to study the active site and catalysis of Pseudomonas aeruginosa phosphorylcholine phosphatase

Beassoni, P.R.; Otero, L.H.; Lisa, A.T.; Domenech, C.E.; Biochim. Biophys. Acta 1784, 2038-2044 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in Escherichia coli ER2566 cells
Pseudomonas aeruginosa
Engineering
Amino acid exchange
Commentary
Organism
D262E
mutant shows activity less than 2% with respect to native recombinant enzyme
Pseudomonas aeruginosa
D267E
mutant shows activity less than 2% with respect to native recombinant enzyme and is not activated by Cu2+
Pseudomonas aeruginosa
S166T
mutant shows activity less than 2% with respect to native recombinant enzyme
Pseudomonas aeruginosa
T35S
mutant shows activity less than 2% with respect to native recombinant enzyme
Pseudomonas aeruginosa
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.4
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
2.5
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
2.6
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
3.2
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
3.5
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
4.3
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
5.1
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
5.4
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
7.6
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
11.5
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
12.2
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
13.1
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
18.7
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
22.2
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Pseudomonas aeruginosa
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cu2+
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+, Cu2+ is able to diminish almost 3times the affinity of the enzyme for p-nitrophenyl with respect to the addition of Zn2+ or Mg2+
Pseudomonas aeruginosa
Mg2+
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+
Pseudomonas aeruginosa
Zn2+
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+
Pseudomonas aeruginosa
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
-
-
-
Purification (Commentary)
Commentary
Organism
-
Pseudomonas aeruginosa
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
75
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
114
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
142
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
Storage Stability
Storage Stability
Organism
-20°C, 10 mM Tris-HCl, pH 8, containing 30% glycerol, more than 1 year, no loss of activity
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-phosphocholine + H2O
-
696420
Pseudomonas aeruginosa
choline + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
-
696420
Pseudomonas aeruginosa
nitrophenol + phosphate
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
0.7
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
1100
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
1400
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
19000
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
21000
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
22000
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
29000
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
120000
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
650000
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
1600000
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
2500000
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
5500000
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
7900000
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli ER2566 cells
Pseudomonas aeruginosa
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D262E
mutant shows activity less than 2% with respect to native recombinant enzyme
Pseudomonas aeruginosa
D267E
mutant shows activity less than 2% with respect to native recombinant enzyme and is not activated by Cu2+
Pseudomonas aeruginosa
S166T
mutant shows activity less than 2% with respect to native recombinant enzyme
Pseudomonas aeruginosa
T35S
mutant shows activity less than 2% with respect to native recombinant enzyme
Pseudomonas aeruginosa
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.4
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
2.5
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
2.6
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
3.2
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
3.5
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
4.3
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
5.1
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
5.4
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
7.6
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
11.5
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
12.2
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
13.1
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
18.7
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
22.2
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
periplasm
-
Pseudomonas aeruginosa
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cu2+
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+, Cu2+ is able to diminish almost 3times the affinity of the enzyme for p-nitrophenyl with respect to the addition of Zn2+ or Mg2+
Pseudomonas aeruginosa
Mg2+
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+
Pseudomonas aeruginosa
Zn2+
activator, the wild type recombinant phosphorylcholine phosphatase has higher affinity for Zn2+ and Cu2+ than for Mg2+
Pseudomonas aeruginosa
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas aeruginosa
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
75
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
114
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
142
-
wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
Storage Stability (protein specific)
Storage Stability
Organism
-20°C, 10 mM Tris-HCl, pH 8, containing 30% glycerol, more than 1 year, no loss of activity
Pseudomonas aeruginosa
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
O-phosphocholine + H2O
-
696420
Pseudomonas aeruginosa
choline + phosphate
-
-
-
?
p-nitrophenyl phosphate + H2O
-
696420
Pseudomonas aeruginosa
nitrophenol + phosphate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.2
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
0.7
-
p-nitrophenyl phosphate
recombinant mutant enzyme D267E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
1100
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
1400
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
19000
-
p-nitrophenyl phosphate
recombinant mutant enzyme D262E, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
21000
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
22000
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
29000
-
p-nitrophenyl phosphate
recombinant mutant enzyme S166T, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
120000
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
650000
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
1600000
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 2 mM Mg2+
Pseudomonas aeruginosa
2500000
-
p-nitrophenyl phosphate
recombinant mutant enzyme T35S, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
5500000
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.5 mM Zn2+
Pseudomonas aeruginosa
7900000
-
p-nitrophenyl phosphate
recombinant wild type enzyme, at pH 5.0 and 37°C, in the presence of 0.3 mM Cu2+
Pseudomonas aeruginosa
Other publictions for EC 3.1.3.75
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)
750176
Huang
Enhanced phosphocholine metab ...
Homo sapiens, Mus musculus
Blood
131
2955-2966
2018
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-
-
-
-
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-
-
-
-
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5
-
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2
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2
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-
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2
2
-
-
-
750211
Morcos
PHOSPHO1 is essential for nor ...
Mus musculus
Bone Joint Res.
7
397-405
2018
-
-
-
-
-
-
-
-
-
-
-
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3
-
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1
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1
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1
1
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751225
Tannert
Pi starvation-dependent regul ...
Arabidopsis thaliana
J. Exp. Bot.
69
467-481
2018
-
-
-
-
-
-
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-
1
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2
-
3
-
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1
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1
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2
-
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1
1
1
1
-
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750663
Pandya
Intravesicular phosphatase PH ...
Mus musculus
Front. Physiol.
8
805
2017
-
-
-
-
-
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-
1
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-
1
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3
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1
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3
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1
1
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-
751205
Zweifler
Role of PHOSPHO1 in periodont ...
Mus musculus
J. Dent. Res.
95
742-751
2016
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2
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1
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1
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-
1
1
-
-
-
749791
Huesa
The functional co-operativity ...
Mus musculus
Biochem. Biophys. Rep.
4
196-201
2015
-
-
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2
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1
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1
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1
1
-
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731455
Bravo
Design, synthesis and evaluati ...
Homo sapiens
Bioorg. Med. Chem. Lett.
24
4308-4311
2014
-
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26
-
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1
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26
-
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26
26
-
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-
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-
-
-
-
-
-
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-
714360
May
Arabidopsis thaliana PECP1 - E ...
Arabidopsis thaliana
Biochim. Biophys. Acta
1824
319-325
2012
-
-
1
-
-
-
-
2
1
5
3
2
-
3
-
-
1
-
-
-
2
1
3
2
-
-
-
2
1
-
-
-
-
1
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-
1
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-
-
-
-
-
-
2
1
5
3
2
-
-
-
1
-
-
2
1
3
2
-
-
-
2
1
-
-
1
-
-
-
-
2
2
714357
Beassoni
Site-directed mutations and ki ...
Pseudomonas aeruginosa
Biochim. Biophys. Acta
1814
858-863
2011
-
-
1
-
3
-
1
4
-
1
-
2
-
4
-
-
-
-
-
-
4
-
3
1
1
-
-
4
1
-
-
-
-
-
-
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-
1
-
-
3
-
-
1
-
4
-
1
-
2
-
-
-
-
-
-
4
-
3
1
1
-
-
4
1
-
-
-
-
1
1
-
4
4
714633
Huesa
PHOSPHO1 is essential for mech ...
Mus musculus
Bone
48
1066-1074
2011
-
-
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1
-
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-
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2
-
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2
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1
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2
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-
-
-
-
-
-
2
2
-
-
-
714872
Domenech
Phosphorylcholine phosphatase: ...
Pseudomonas aeruginosa
Enzyme Res.
2011
561841
2011
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