BRENDA - Enzyme Database
show all sequences of 4.6.1.13

Investigating the interfacial binding of bacterial phosphatidylinositol-specific phospholipase C

Wehbi, H.; Feng, J.; Kolbeck, J.; Ananthanarayanan, B.; Cho, W.; Roberts, M.F.; Biochemistry 42, 9374-9382 (2003)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
phosphatidic acid
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylcholine
binding to nonsubstrate zwitterionic phosphatidylcholine interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylglycerol
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylmethanol
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylserine
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
Cloned(Commentary)
Commentary
Organism
wild-type and mutant PI-PLC, expression in Escherichia coli BL21
Bacillus thuringiensis
Engineering
Amino acid exchange
Commentary
Organism
K44A
interfacial binding study
Bacillus thuringiensis
R69D
active site mutant with low specific activity towards phosphatidylinositol, interfacial binding study
Bacillus thuringiensis
W242A
interfacial binding study
Bacillus thuringiensis
W47A
interfacial binding study
Bacillus thuringiensis
W47A/W242A
double mutant, interfacial binding study
Bacillus thuringiensis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus thuringiensis
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant PI-PLC
Bacillus thuringiensis
Reaction
Reaction
Commentary
Organism
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol
general acid/general base mechanism
Bacillus thuringiensis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Bacillus thuringiensis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-phosphatidyl-1D-myo-inositol
general acid/general base mechanism, enhanced activity when phosphatidylinositol is present in an interface compared to monomeric substrate
650231
Bacillus thuringiensis
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
PI-PLC catalyzes the hydrolysis of myo-inositol 1,2-cyclic phosphate to myo-inositol 1-phosphate
650231
Bacillus thuringiensis
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.1
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine
Bacillus thuringiensis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
8
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine, drop in activity around pH 8, consistent with the drop in binding affinity for activating surfaces
Bacillus thuringiensis
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Bacillus thuringiensis
theoretical pI
-
5.4
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
phosphatidic acid
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylcholine
binding to nonsubstrate zwitterionic phosphatidylcholine interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylglycerol
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylmethanol
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
phosphatidylserine
binding to nonsubstrate anionic interfaces enhances the catalytic activity of PI-PLC, interfacial binding studies, activation mechanism
Bacillus thuringiensis
Cloned(Commentary) (protein specific)
Commentary
Organism
wild-type and mutant PI-PLC, expression in Escherichia coli BL21
Bacillus thuringiensis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K44A
interfacial binding study
Bacillus thuringiensis
R69D
active site mutant with low specific activity towards phosphatidylinositol, interfacial binding study
Bacillus thuringiensis
W242A
interfacial binding study
Bacillus thuringiensis
W47A
interfacial binding study
Bacillus thuringiensis
W47A/W242A
double mutant, interfacial binding study
Bacillus thuringiensis
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant PI-PLC
Bacillus thuringiensis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Bacillus thuringiensis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-phosphatidyl-1D-myo-inositol
general acid/general base mechanism, enhanced activity when phosphatidylinositol is present in an interface compared to monomeric substrate
650231
Bacillus thuringiensis
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol
PI-PLC catalyzes the hydrolysis of myo-inositol 1,2-cyclic phosphate to myo-inositol 1-phosphate
650231
Bacillus thuringiensis
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.1
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine
Bacillus thuringiensis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
8
-
cleavage of phosphatidylinositol solubilized in diheptanoyl phosphatidylcholine, drop in activity around pH 8, consistent with the drop in binding affinity for activating surfaces
Bacillus thuringiensis
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Bacillus thuringiensis
theoretical pI
-
5.4
Other publictions for EC 4.6.1.13
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)
729401
Cheng
Does changing the predicted dy ...
Bacillus thuringiensis, Bacillus thuringiensis N168C
Biophys. J.
104
185-195
2013
1
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1
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1
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729893
Grauffel
Cation-pi interactions as lipi ...
Bacillus thuringiensis, Bacillus thuringiensis N168C
J. Am. Chem. Soc.
135
5740-5750
2013
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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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4
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1
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1
2
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1
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2
1
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1
1
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729728
Rupwate
Regulation of lipid biosynthes ...
Oryza sativa
FEBS Lett.
586
1555-1560
2012
-
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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
1
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730001
Cheng
Competition between anion bind ...
Staphylococcus aureus
J. Biol. Chem.
287
40317-40327
2012
-
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1
1
10
-
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1
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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1
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1
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1
10
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1
1
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1
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1
1
1
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1
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-
-
2
2
-
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-
708443
Almeida-Amaral
Leishmania amazonensis: heme s ...
Leishmania amazonensis
Exp. Parasitol.
124
436-441
2010
1
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2
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2
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1
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2
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1
1
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-
708878
Bai
Unique catalytic mechanism of ...
Streptomyces antibioticus
J. Am. Chem. Soc.
132
1210-1211
2010
-
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1
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3
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710429
Davies
The alpha2delta subunits of vo ...
synthetic construct
Proc. Natl. Acad. Sci. USA
107
1654-1659
2010
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1
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1
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1
1
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-
691015
Chen
Listeria monocytogenes phospha ...
Listeria monocytogenes
Biochemistry
48
3578-3592
2009
1
-
1
-
5
-
-
-
-
-
3
-
-
1
-
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1
-
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1
3
1
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1
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1
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5
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3
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1
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1
3
1
-
-
-
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-
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-
-
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-
-
-
-
-
694020
Poussin
The ability of Listeria monocy ...
Listeria monocytogenes 10403S, Listeria monocytogenes
Microb. Pathog.
46
1-5
2009
-
-
-
-
4
-
-
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1
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2
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2
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4
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1
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2
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-
-
-
-
-
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-
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707504
Pu
Fluorescence correlation spect ...
Bacillus thuringiensis
Biochemistry
48
6835-6845
2009
1
1
1
-
7
-
-
-
-
-
-
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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
1
1
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7
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1
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1
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2
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1
1
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-
708374
Kloeppel
Two isoforms of eukaryotic pho ...
Paramecium tetraurelia, Paramecium tetraurelia d4-2
Eur. J. Cell Biol.
88
577-592
2009
2
-
1
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1
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3
-
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1
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2
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2
1
1
2
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-
709019
Shi
Modulation of Bacillus thuring ...
Bacillus thuringiensis
J. Biol. Chem.
284
15607-15618
2009
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1
1
4
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1
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1
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20
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1
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1
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1
4
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1
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20
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1
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690951
Guo
Role of helix B residues in in ...
Bacillus thuringiensis
Biochemistry
47
4201-4210
2008
1
-
1
-
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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1
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11
-
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1
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-
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1
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-
-
-
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-
-
-
-
668921
Poussin
Involvement of Listeria monocy ...
Listeria monocytogenes
Infect. Immun.
73
4410-4413
2005
-
-
-
-
-
-
-
-
-
-
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1
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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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668926
Wei
Characterization of Listeria m ...
Bacillus anthracis
Infect. Immun.
73
6639-6646
2005
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1
-
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-
-
-
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1
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1
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2
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669722
Zenewicz
Phosphatidylinositol-specific ...
Bacillus anthracis
J. Immunol.
174
8011-8016
2005
-
-
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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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670672
Wei
Listeria monocytogenes phospha ...
Listeria monocytogenes
Proc. Natl. Acad. Sci. USA
102
12927-12931
2005
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-
-
-
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1
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1
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1
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1
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652552
Zhao
The catalytic role of aspartat ...
Bacillus thuringiensis
J. Biol. Chem.
279
31995-32000
2004
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1
4
-
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1
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1
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1
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1
1
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1
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1
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2
1
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1
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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1
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-
-
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2
1
-
-
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-
-
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-
670066
Ikezawa
-
Bacterial phosphatidylinositol ...
Bacillus cereus, Bacillus thuringiensis, Listeria monocytogenes, Staphylococcus aureus
J. Toxicol. Toxin Rev.
23
479-508
2004
-
3
-
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1
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2
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4
-
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1
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6
-
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3
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1
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2
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1
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6
-
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650204
Kravchuk
Engineering a catalytic metal ...
Bacillus sp. (in: Bacteria)
Biochemistry
42
2422-2430
2003
-
-
-
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7
-
4
-
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8
-
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1
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1
1
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2
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1
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1
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1
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7
-
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4
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8
-
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1
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2
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1
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1
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1
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650231
Wehbi
Investigating the interfacial ...
Bacillus thuringiensis
Biochemistry
42
9374-9382
2003
5
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1
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5
-
-
-
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Mechanism of phosphatidylinosi ...
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A catalytic diad involved in s ...
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285241
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Purification and properties of ...
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High-level expression in Esche ...
Bacillus cereus, Bacillus thuringiensis
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1991
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Taguchi
Purification and properties of ...
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Sundler
Enzymatic properties of phosph ...
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Ikezawa
Studies on phosphatidylinosito ...
Bacillus cereus
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