BRENDA - Enzyme Database
show all sequences of 5.4.99.5

Evolution of allosteric regulation in chorismate mutases from early plants

Kroll, K.; Holland, C.K.; Starks, C.M.; Jez, J.M.; Biochem. J. 474, 3705-3717 (2017)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
cysteine
-
Arabidopsis thaliana
histidine
is a positive effector for the enzyme
Amborella trichopoda
histidine
is a positive effector for the enzyme
Physcomitrella patens
histidine
-
Arabidopsis thaliana
additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
Arabidopsis thaliana
additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
Selaginella moellendorffii
tryptophan
is a positive effector for the enzyme; is a positive effector for the enzyme
Amborella trichopoda
tryptophan
-
Arabidopsis thaliana
tryptophan
is a positive effector for the enzyme; is a positive effector for the enzyme, identification of the allosteric effector site and the structural differences between the R- (more active) and T-state (less active) forms of plant chorismate mutase
Physcomitrella patens
tryptophan
is a positive effector for the enzyme
Selaginella moellendorffii
Cloned(Commentary)
Commentary
Organism
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
Selaginella moellendorffii
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3); sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
Amborella trichopoda
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3); sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
Physcomitrella patens
sequence comparisons; sequence comparisons; sequence comparisons
Arabidopsis thaliana
Crystallization (Commentary)
Crystallization
Organism
purified recombinant detagged isozyme PpCM1 in complex with tryptophan, hanging drop vapor diffusion method, mixing of 0.001 ml of 6 mg/ml proteinin 25 mM HEPES, pH 7.5, and 100 mM NaCl with 0.001 ml of reservoir solution containing 10% w/v PEG 4000, 20% v/v 2-propanol, and 100 mM HEPES, pH 7.5, at 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement using Arabidopsis thaliana isozyme AtCM1 in complex with tyrosine structure (PDB ID 4PPU) as search model, modeling
Physcomitrella patens
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
Selaginella moellendorffii
tyrosine
is a negative effector for the enzyme; is a negative effector for the enzyme
Amborella trichopoda
tyrosine
is a negative effector for the enzyme; is a negative effector for the enzyme
Physcomitrella patens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten steady-state kinetics; Michaelis-Menten steady-state kinetics
Amborella trichopoda
additional information
-
additional information
Michaelis-Menten steady-state kinetics; Michaelis-Menten steady-state kinetics
Physcomitrella patens
additional information
-
additional information
Michaelis-Menten steady-state kinetics
Selaginella moellendorffii
2.33
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
2.39
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
3.19
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
5.19
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Selaginella moellendorffii
6.79
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
identification of a chloroplast transit peptide; identification of a chloroplast transit peptide
Amborella trichopoda
9507
-
chloroplast
identification of a chloroplast transit peptide; identification of a chloroplast transit peptide
Physcomitrella patens
9507
-
chloroplast
;
Arabidopsis thaliana
9507
-
cytosol
-
Arabidopsis thaliana
5829
-
additional information
enzyme SmCM is not predicted to have a chloroplast signal peptide
Selaginella moellendorffii
-
-
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
about, recombinant detagged enzyme, gel filtration; about, recombinant detagged enzyme, gel filtration
Amborella trichopoda
60000
-
about, recombinant detagged enzyme, gel filtration; about, recombinant detagged enzyme, gel filtration
Physcomitrella patens
60000
-
about, recombinant detagged enzyme, gel filtration
Selaginella moellendorffii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
Chorismate
Physcomitrella patens
-
Prephenate
-
-
?
Chorismate
Selaginella moellendorffii
-
Prephenate
-
-
?
Chorismate
Amborella trichopoda
-
Prephenate
-
-
?
Chorismate
Arabidopsis thaliana
-
Prephenate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Amborella trichopoda
U5D896
-
-
Amborella trichopoda
W1PFX5
-
-
Arabidopsis thaliana
P42738
-
-
Arabidopsis thaliana
Q9C544
-
-
Arabidopsis thaliana
Q9S7H4
-
-
Physcomitrella patens
A0A2K1JMA3
-
-
Physcomitrella patens
A9S498
-
-
Selaginella moellendorffii
D8R1Y1
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration
Selaginella moellendorffii
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration; recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration
Amborella trichopoda
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration; recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration
Physcomitrella patens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
enzyme activity in presence of amino acid effectors, overview; enzyme activity in presence of amino acid effectors, overview
Amborella trichopoda
additional information
-
enzyme activity in presence of amino acid effectors, overview; enzyme activity in presence of amino acid effectors, overview
Physcomitrella patens
additional information
-
enzyme activity in presence of amino acid effectors, overview
Selaginella moellendorffii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Chorismate
-
747032
Physcomitrella patens
Prephenate
-
-
-
?
Chorismate
-
747032
Selaginella moellendorffii
Prephenate
-
-
-
?
Chorismate
-
747032
Amborella trichopoda
Prephenate
-
-
-
?
Chorismate
-
747032
Arabidopsis thaliana
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Physcomitrella patens
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Selaginella moellendorffii
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Amborella trichopoda
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Arabidopsis thaliana
Prephenate
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE; 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
Amborella trichopoda
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE; 2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
Physcomitrella patens
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
Selaginella moellendorffii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Arabidopsis thaliana
15
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
16
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Arabidopsis thaliana
18.8
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Selaginella moellendorffii
19.5
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
20.7
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
22.8
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
39
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Arabidopsis thaliana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at; assay at
Amborella trichopoda
8
-
assay at
Arabidopsis thaliana
8
-
assay at; assay at
Physcomitrella patens
8
-
assay at
Selaginella moellendorffii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
cysteine
-
Arabidopsis thaliana
histidine
is a positive effector for the enzyme
Amborella trichopoda
histidine
-
Arabidopsis thaliana
histidine
is a positive effector for the enzyme
Physcomitrella patens
additional information
isozyme AtCM3 is unaltered by either phenylalanine or tyrosine but is activated by tryptophan, histidine, and cysteine
Arabidopsis thaliana
additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
Selaginella moellendorffii
tryptophan
is a positive effector for the enzyme
Amborella trichopoda
tryptophan
-
Arabidopsis thaliana
tryptophan
is a positive effector for the enzyme, identification of the allosteric effector site and the structural differences between the R- (more active) and T-state (less active) forms of plant chorismate mutase
Physcomitrella patens
tryptophan
is a positive effector for the enzyme
Physcomitrella patens
tryptophan
is a positive effector for the enzyme
Selaginella moellendorffii
Cloned(Commentary) (protein specific)
Commentary
Organism
sequence comparisons
Arabidopsis thaliana
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
Amborella trichopoda
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
Physcomitrella patens
sequence comparisons, recombinant expression of codon-optimized N-terminally His6-tagged enzyme in Escherichia coli strain Rosetta II (DE3)
Selaginella moellendorffii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant detagged isozyme PpCM1 in complex with tryptophan, hanging drop vapor diffusion method, mixing of 0.001 ml of 6 mg/ml proteinin 25 mM HEPES, pH 7.5, and 100 mM NaCl with 0.001 ml of reservoir solution containing 10% w/v PEG 4000, 20% v/v 2-propanol, and 100 mM HEPES, pH 7.5, at 4°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement using Arabidopsis thaliana isozyme AtCM1 in complex with tyrosine structure (PDB ID 4PPU) as search model, modeling
Physcomitrella patens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
neither tyrosine nor phenylalanine alters the activity of enzyme SmCM
Selaginella moellendorffii
tyrosine
is a negative effector for the enzyme
Amborella trichopoda
tyrosine
is a negative effector for the enzyme
Physcomitrella patens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten steady-state kinetics
Amborella trichopoda
additional information
-
additional information
Michaelis-Menten steady-state kinetics
Physcomitrella patens
additional information
-
additional information
Michaelis-Menten steady-state kinetics
Selaginella moellendorffii
2.33
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
2.39
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
3.19
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
5.19
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Selaginella moellendorffii
6.79
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
identification of a chloroplast transit peptide
Amborella trichopoda
9507
-
chloroplast
identification of a chloroplast transit peptide
Physcomitrella patens
9507
-
chloroplast
-
Arabidopsis thaliana
9507
-
cytosol
-
Arabidopsis thaliana
5829
-
additional information
enzyme SmCM is not predicted to have a chloroplast signal peptide
Selaginella moellendorffii
-
-
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
60000
-
about, recombinant detagged enzyme, gel filtration
Amborella trichopoda
60000
-
about, recombinant detagged enzyme, gel filtration
Physcomitrella patens
60000
-
about, recombinant detagged enzyme, gel filtration
Selaginella moellendorffii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
Chorismate
Physcomitrella patens
-
Prephenate
-
-
?
Chorismate
Selaginella moellendorffii
-
Prephenate
-
-
?
Chorismate
Amborella trichopoda
-
Prephenate
-
-
?
Chorismate
Arabidopsis thaliana
-
Prephenate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration
Amborella trichopoda
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration
Physcomitrella patens
recombinant His6-tagged enzyme from Escherichia coli strain Rosetta II (DE3) by nickel affinity chromatography, tag cleavage with thrombin, dialysis, another step of nickel affinity chromatography, dialysis, and gel filtration
Selaginella moellendorffii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
enzyme activity in presence of amino acid effectors, overview
Amborella trichopoda
additional information
-
enzyme activity in presence of amino acid effectors, overview
Physcomitrella patens
additional information
-
enzyme activity in presence of amino acid effectors, overview
Selaginella moellendorffii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Chorismate
-
747032
Physcomitrella patens
Prephenate
-
-
-
?
Chorismate
-
747032
Selaginella moellendorffii
Prephenate
-
-
-
?
Chorismate
-
747032
Amborella trichopoda
Prephenate
-
-
-
?
Chorismate
-
747032
Arabidopsis thaliana
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Physcomitrella patens
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Selaginella moellendorffii
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Amborella trichopoda
Prephenate
-
-
-
?
Chorismate
interactions with charged residues in the active site distort chorismate into a reactive transition state that leads to prephenate
747032
Arabidopsis thaliana
Prephenate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
Amborella trichopoda
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
Physcomitrella patens
homodimer
2 * 28000-30000, recombinant detagged enzyme, SDS-PAGE
Selaginella moellendorffii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Arabidopsis thaliana
15
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
16
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Arabidopsis thaliana
18.8
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Selaginella moellendorffii
19.5
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
20.7
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
22.8
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
39
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Arabidopsis thaliana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Amborella trichopoda
8
-
assay at
Arabidopsis thaliana
8
-
assay at
Physcomitrella patens
8
-
assay at
Selaginella moellendorffii
Expression
Organism
Commentary
Expression
Amborella trichopoda
the isozyme AtmCM2 is downregulated by phenylalanine
down
General Information
General Information
Commentary
Organism
evolution
evolution of allosteric regulation in plant chorismate mutases, overview; evolution of allosteric regulation in plant chorismate mutases, overview
Amborella trichopoda
evolution
analysis of evolution of allosteric regulation in plant chorismate mutases; analysis of evolution of allosteric regulation in plant chorismate mutases; analysis of evolution of allosteric regulation in plant chorismate mutases. Phylogentically, the AtCM3-like clade is found only in the Brassicaceae, which suggests a possible specialized role for this enzyme in those plants
Arabidopsis thaliana
evolution
evolution of allosteric regulation in plant chorismate mutases, overview; evolution of allosteric regulation in plant chorismate mutases, overview
Physcomitrella patens
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
Selaginella moellendorffii
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid; anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
Amborella trichopoda
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid; anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid; anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
Arabidopsis thaliana
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid buildup of the amino acid; anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid buildup of the amino acid
Physcomitrella patens
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
Selaginella moellendorffii
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview; structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
Amborella trichopoda
additional information
isozyme PpCM1 structure-function analysis, structure comparisons, active site and allosteric effector sites of PpCM1, targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview; structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
Physcomitrella patens
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
Selaginella moellendorffii
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview; chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
Amborella trichopoda
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The cytosolic chorismate mutase isozyme AtCM2 is unregulated; chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM1 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis; chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM3 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis
Arabidopsis thaliana
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen re-arrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview; chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen re-arrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
Physcomitrella patens
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
Selaginella moellendorffii
General Information (protein specific)
General Information
Commentary
Organism
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
Amborella trichopoda
evolution
analysis of evolution of allosteric regulation in plant chorismate mutases
Arabidopsis thaliana
evolution
analysis of evolution of allosteric regulation in plant chorismate mutases. Phylogentically, the AtCM3-like clade is found only in the Brassicaceae, which suggests a possible specialized role for this enzyme in those plants
Arabidopsis thaliana
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
Physcomitrella patens
evolution
evolution of allosteric regulation in plant chorismate mutases, overview
Selaginella moellendorffii
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
Amborella trichopoda
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
Arabidopsis thaliana
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid buildup of the amino acid
Physcomitrella patens
metabolism
anthranilate synthase competes with chorismate mutase for chorismate for the tryptophan biosynthetic pathway. The two enzymes of this branch point are reciprocally regulated by feedback activation and/or inhibition in higher plants. For example, tryptophan inhibits anthranilate synthase and activates chorismate mutase to avoid build up of the amino acid
Selaginella moellendorffii
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
Amborella trichopoda
additional information
isozyme PpCM1 structure-function analysis, structure comparisons, active site and allosteric effector sites of PpCM1, targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
Physcomitrella patens
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
Physcomitrella patens
additional information
structure comparisons and targeted sequence alignment of allosteric effector site residues of the chorismate mutases, overview
Selaginella moellendorffii
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
Amborella trichopoda
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM1 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis
Arabidopsis thaliana
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The cytosolic chorismate mutase isozyme AtCM2 is unregulated
Arabidopsis thaliana
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. The plastid-localized chorismate mutase isozyme AtCM3 is allosterically regulated. The allosterically regulated chorismate mutases are repressed by tyrosine and phenylalanine and are activated by tryptophan. The aromatic amino acids bind an effector site on the enzyme and regulate the ability of chorismate to bind at the active site for catalysis
Arabidopsis thaliana
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen re-arrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
Physcomitrella patens
physiological function
chorismate lies at the metabolic branch point of aromatic amino acid biosynthesis, where chorismate mutase catalyzes the pericyclic Claisen rearrangement of chorismate into prephenate in the first committed step of phenylalanine and tyrosine biosynthesis. Allosteric regulation of plant enzymes, overview
Selaginella moellendorffii
Expression (protein specific)
Organism
Commentary
Expression
Amborella trichopoda
the isozyme AtmCM2 is downregulated by phenylalanine
down
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.36
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
3.62
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Selaginella moellendorffii
4.7
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
8.34
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
8.66
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3.36
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
3.62
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Selaginella moellendorffii
4.7
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Amborella trichopoda
8.34
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
8.66
-
chorismate
pH 8.0, temperature not specified in the publication, recombinant enzyme
Physcomitrella patens
Other publictions for EC 5.4.99.5
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)
746674
Asojo
Crystal structure of chorisma ...
Paraburkholderia phymatum, Paraburkholderia phymatum DSM 17167 / CIP 108236 / LMG 21445 / STM815
Acta Crystallogr. Sect. F
74
187-192
2018
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1
1
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2
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8
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2
1
-
-
-
-
-
-
-
-
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2
2
-
-
-
746675
Asojo
Crystal structure of chorisma ...
Burkholderia thailandensis, Burkholderia thailandensis ATCC 700388 / DSM 13276 / CIP 106301 / E264
Acta Crystallogr. Sect. F
74
294-299
2018
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1
1
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2
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5
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2
1
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-
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1
1
-
-
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747338
Wu
Enhancement of L-phenylalanin ...
Escherichia coli
Biotechnol. Appl. Biochem.
65
476-483
2018
-
1
-
-
-
-
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3
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1
1
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-
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747032
Kroll
Evolution of allosteric regul ...
Amborella trichopoda, Arabidopsis thaliana, Physcomitrella patens, Selaginella moellendorffii
Biochem. J.
474
3705-3717
2017
10
-
4
1
-
-
3
8
5
-
3
8
-
10
-
-
3
-
-
-
3
-
16
3
-
-
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8
4
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12
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8
-
1
-
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5
-
10
8
-
5
8
-
-
-
5
-
-
5
-
16
5
-
-
-
8
6
-
-
-
1
15
29
1
5
5
747259
Khanapur
Mycobacterium tuberculosis ch ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv
Bioorg. Med. Chem.
25
1725-1736
2017
-
1
1
-
-
-
35
2
1
-
-
2
-
7
-
-
-
-
-
-
-
-
6
2
1
-
1
1
1
-
-
-
4
-
7
-
1
1
-
-
-
-
7
35
4
2
1
-
-
2
-
-
-
-
-
-
-
-
6
2
1
-
1
1
1
-
-
-
-
4
4
-
1
1
749355
Pratap
Structure of chorismate mutas ...
Bacillus subtilis 168, Bacillus subtilis
Sci. Rep.
7
6364
2017
-
-
1
1
-
-
2
3
-
-
-
4
-
5
-
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1
-
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1
1
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2
1
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1
-
1
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4
-
4
-
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4
-
-
-
1
-
-
-
-
4
1
2
-
-
2
2
-
-
-
-
3
6
-
2
2
747842
Perez
The importance of chorismate ...
Trichoderma parareesei, Trichoderma parareesei IMI 113135 / T6
Front. Microbiol.
6
1181
2015
-
-
1
-
1
-
-
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10
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1
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1
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1
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1
-
-
-
-
1
-
-
-
1
-
-
-
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3
3
-
-
-
747499
Jeankumar
Discovery and structure optim ...
Mycobacterium tuberculosis
Chem. Biol. Drug Des.
83
498-506
2014
-
-
-
-
-
-
34
-
-
-
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1
-
2
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1
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29
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29
34
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1
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1
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-
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-
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-
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-
748178
Westfall
Structural evolution of diffe ...
Arabidopsis thaliana
J. Biol. Chem.
289
28619-28628
2014
4
-
1
1
9
-
3
4
2
-
1
3
-
7
-
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1
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-
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3
1
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3
1
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5
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3
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1
9
-
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3
-
6
3
-
3
3
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3
-
-
-
-
3
3
-
-
-
3
3
-
-
-
-
2
6
-
3
3
748301
Alokam
Identification and structure- ...
Mycobacterium tuberculosis
J. Enzyme Inhib. Med. Chem.
29
547-554
2014
-
1
-
-
-
-
19
-
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1
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3
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1
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15
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1
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15
19
1
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1
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2
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1
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-
-
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1
1
-
-
-
749167
Burschowsky
Electrostatic transition stat ...
Bacillus subtilis
Proc. Natl. Acad. Sci. USA
111
17516-17521
2014
-
-
1
1
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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2
2
-
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749298
Hu
-
Wild-type and molten globular ...
Meloidogyne javanica
Sci. China Chem.
57
156-164
2014
-
-
-
-
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1
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2
2
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-
714917
Yu
-
Chorismate mutase: An alternat ...
Globodera pallida, Globodera rostochiensis, Globodera tabacum
Eur. J. Plant Pathol.
129
89-102
2011
-
-
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716409
Claeyssens
Analysis of chorismate mutase ...
Bacillus subtilis
Org. Biomol. Chem.
9
1578-1590
2011
-
-
-
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716951
Ferrer
-
Molecular mechanism of chorism ...
Mycobacterium tuberculosis
Theoret. Chem. Accounts
128
601-607
2011
-
-
-
-
-
-
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1
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-
-
-
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726963
Lamb
Pericyclic reactions catalyzed ...
Pseudomonas aeruginosa
Biochemistry
50
7476-7483
2011
-
-
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1
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2
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704211
Ishida
Effects of point mutation on e ...
Bacillus subtilis
J. Am. Chem. Soc.
132
7104-7118
2010
-
-
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706137
Degrassi
Xanthomonas oryzae pv. oryzae ...
Xanthomonas oryzae
Phytopathology
100
262-270
2010
-
-
-
-
-
-
-
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3
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4
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1
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2
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1
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1
1
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706241
Colquhoun
A petunia chorismate mutase sp ...
Petunia x hybrida
Plant J.
61
145-155
2010
1
-
1
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3
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5
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2
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-
-
2
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1
1
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706631
Mueller
Design, selection, and charact ...
Methanocaldococcus jannaschii
Protein Sci.
19
1000-1010
2010
-
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1
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2
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692260
Lim
Characterization of a key trif ...
Archaeoglobus fulgidus
Extremophiles
13
191-198
2009
-
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1
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1
1
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3
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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1
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1
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-
701494
Okvist
A novel noncovalent complex of ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
65
1048-1052
2009
1
-
1
1
-
-
-
-
-
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7
-
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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
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703449
Sasso
Structure and function of a co ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
EMBO J.
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2009
2
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1
1
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3
2
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
5
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3
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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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2
2
705570
Li
Genetic and biochemical identi ...
Corynebacterium glutamicum
Microbiology
155
3382-3391
2009
1
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1
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3
1
1
1
3
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4
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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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1
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3
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1
1
1
3
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-
-
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1
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-
-
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1
1
-
-
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1
-
-
-
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2
2
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705812
Hu
Functional contribution of cho ...
Hordeum vulgare
Mol. Plant Microbe Interact.
22
311-320
2009
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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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-
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-
-
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1
1
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705814
Vanholme
Structural and functional inve ...
Heterodera schachtii
Mol. Plant Pathol.
10
189-200
2009
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1
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1
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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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2
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2
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706236
Tzin
Expression of a bacterial bi-f ...
Escherichia coli
Plant J.
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2009
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1
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1
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1
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-
-
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1
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-
-
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-
-
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1
1
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674346
Schneider
The two chorismate mutases fro ...
Mycobacterium tuberculosis, Mycolicibacterium smegmatis, no activity in Corynebacterium diphtheriae, no activity in Mycobacterium leprae, no activity in Nocardia farcinica
J. Bacteriol.
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2008
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1
2
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3
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1
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1
1
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-
-
-
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-
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1
1
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1
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-
-
-
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1
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2
2
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-
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1
-
-
-
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3
-
1
-
-
1
1
-
-
-
-
-
-
-
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-
684578
Chavez-Bejar
Metabolic engineering of Esche ...
Escherichia coli, Escherichia coli JM101
Appl. Environ. Microbiol.
74
3284-3290
2008
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1
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11
-
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2
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-
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-
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-
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-
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1
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-
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-
-
-
-
-
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-
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2
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-
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-
-
-
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-
-
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690920
Woycechowsky
Relative tolerance of an enzym ...
Methanocaldococcus jannaschii
Biochemistry
47
13489-13496
2008
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1
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5
-
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6
-
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-
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1
-
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1
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1
1
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6
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-
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1
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5
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6
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-
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-
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1
-
-
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1
1
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-
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6
-
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692314
Kim
A comparative biochemical and ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Yersinia pestis
FEBS J.
275
4824-4835
2008
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2
2
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3
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3
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2
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3
2
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-
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2
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-
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-
-
2
-
2
-
-
-
-
-
2
3
-
3
-
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2
-
-
-
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3
2
-
-
-
2
-
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-
-
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693664
Vamvaca
Kinetics and thermodynamics of ...
Methanocaldococcus jannaschii
J. Mol. Biol.
382
971-977
2008
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1
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1
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-
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1
2
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-
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2
-
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-
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1
-
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-
-
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1
2
-
-
-
-
-
-
-
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1
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
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694070
Lu
Alternative splicing: A novel ...
Globodera rostochiensis
Mol. Biochem. Parasitol.
162
1-15
2008
1
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1
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1
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1
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8
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1
-
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1
1
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-
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-
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-
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1
-
1
-
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1
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-
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-
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1
-
-
-
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-
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1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
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694875
Roca
On the relationship between fo ...
Methanocaldococcus jannaschii
Proc. Natl. Acad. Sci. USA
105
13877-13882
2008
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-
1
-
-
-
-
-
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-
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1
-
-
-
-
-
-
-
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1
2
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-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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-
-
-
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-
-
-
-
-
-
-
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1
2
-
-
-
-
-
-
-
-
-
-
-
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672268
Lassila
Exhaustive mutagenesis of six ...
Escherichia coli
Biochemistry
46
6883-6891
2007
-
1
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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-
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1
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1
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1
1
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-
-
-
-
-
-
-
1
1
-
-
1
-
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-
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1
-
-
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1
-
-
-
1
-
-
-
-
1
-
1
-
1
1
-
-
-
-
-
-
-
-
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672622
Agrawal
Ligand based virtual screening ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Bioorg. Med. Chem. Lett.
17
3053-3058
2007
-
1
-
1
-
-
8
1
1
-
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1
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7
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
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4
-
3
-
1
-
-
1
-
-
3
8
4
1
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
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1
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675620
Crehuet
A transition path sampling stu ...
Bacillus subtilis
J. Phys. Chem. B
111
5708-5718
2007
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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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1
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-
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-
-
-
-
-
-
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-
-
-
-
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-
1
-
-
-
-
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1
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-
-
-
-
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1
-
-
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662663
Kong
The allosteric mechanism of ye ...
Saccharomyces cerevisiae
J. Mol. Biol.
356
237-247
2006
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1
2
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1
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2
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1
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-
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-
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-
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1
2
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1
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-
-
-
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1
-
-
-
-
-
-
-
-
-
-
-
-
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-
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671111
Krengel
Preliminary X-ray crystallogra ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
62
441-445
2006
-
-
1
1
-
-
-
-
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1
1
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8
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-
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-
-
-
-
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1
1
1
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-
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1
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1
-
1
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1
1
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-
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-
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1
1
1
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-
1
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672183
Qamra
The 2.15 A crystal structure o ...
Mycobacterium tuberculosis
Biochemistry
45
6997-7005
2006
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1
1
1
-
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2
-
2
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1
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4
-
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1
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-
-
-
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1
2
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1
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-
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-
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1
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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1
2
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1
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672198
Zhang
Temperature dependence of the ...
Thermus thermophilus
Biochemistry
45
8562-8567
2006
-
-
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1
-
-
-
-
-
-
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1
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3
-
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1
-
-
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1
1
2
1
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-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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1
-
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-
-
-
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1
1
2
1
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674312
Kim
Biochemical and structural cha ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Bacteriol.
188
8638-8648
2006
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1
1
1
9
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1
2
1
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2
1
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8
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1
1
-
-
-
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1
1
1
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1
1
1
-
-
-
-
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1
1
-
1
9
-
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1
-
2
1
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2
1
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1
-
-
-
-
1
1
1
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-
1
1
1
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675369
Okvist
1.6 A crystal structure of the ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Mol. Biol.
357
1483-1499
2006
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1
1
1
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7
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1
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1
2
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1
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1
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-
-
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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
2
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1
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1
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675611
Ishida
All electron quantum chemical ...
Bacillus subtilis
J. Phys. Chem. B
110
1457-1463
2006
1
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1
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3
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1
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1
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2
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1
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-
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1
-
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1
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-
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-
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1
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1
-
2
-
-
-
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1
-
-
-
-
-
-
-
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-
660628
Qamra
Crystallization and preliminar ...
Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
F61
473-475
2005
-
1
1
1
-
-
1
-
-
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1
1
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6
-
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1
-
-
-
-
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1
1
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-
-
-
-
-
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1
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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-
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1
1
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-
-
-
-
-
-
-
-
-
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661158
Zhang
A definitive mechanism for cho ...
Escherichia coli
Biochemistry
44
10443-10448
2005
-
-
-
1
-
-
-
-
-
-
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1
-
2
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-
-
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-
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1
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-
-
-
-
-
-
-
-
-
-
-
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-
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1
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1
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-
-
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1
-
-
-
-
-
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661703
Sasso
Characterization of the secret ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
FEBS J.
272
375-389
2005
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1
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2
2
2
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2
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1
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1
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2
1
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1
2
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1
1
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1
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2
1
2
2
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6
2
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1
1
-
-
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2
1
-
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1
2
-
-
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1
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662365
Prakash
Purified recombinant hypotheti ...
Mycobacterium tuberculosis
J. Biol. Chem.
280
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2005
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1
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-
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1
2
1
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1
1
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5
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1
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-
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2
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1
1
-
1
1
1
1
1
-
-
-
-
-
-
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1
-
-
-
-
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1
-
2
1
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1
1
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1
-
-
2
-
1
1
-
1
1
1
1
1
-
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662707
Marti
Computing kinetic isotope effe ...
Bacillus subtilis
J. Phys. Chem. B
109
3707-3710
2005
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-
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1
1
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1
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2
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1
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-
-
-
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-
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-
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1
1
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1
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-
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-
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1
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-
-
-
-
-
-
-
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662923
Huang
Two chorismate mutase genes fr ...
Meloidogyne incognita
Mol. Plant Pathol.
6
23-30
2005
-
1
1
-
-
-
-
-
-
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9
-
-
-
-
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1
-
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-
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-
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-
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1
1
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-
-
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-
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-
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1
-
-
-
-
-
-
-
-
-
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-
-
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663240
Zhang
The proficiency of a thermophi ...
Thermus thermophilus
Proc. Natl. Acad. Sci. USA
102
18356-18360
2005
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1
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-
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1
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2
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1
1
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-
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-
-
-
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1
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1
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-
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1
1
-
-
-
-
-
-
-
-
-
-
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-
663283
Lassila
Computationally designed varia ...
Escherichia coli
Protein Eng. Des. Sel.
18
161-163
2005
-
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1
1
5
-
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5
-
-
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1
-
2
-
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1
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-
-
-
-
1
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-
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5
-
-
-
-
-
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-
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1
-
1
5
-
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-
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5
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1
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Chorismate mutase inhibitors: ...
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J. Org. Chem.
53
3195-3210
1988
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3566
Ahmad
Chorismate mutase: prephenate ...
Acinetobacter calcoaceticus
Eur. J. Biochem.
176
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1988
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3555
Görisch
Chorismate mutase from Strepto ...
Kitasatospora aureofaciens, Streptomyces venezuelae
Methods Enzymol.
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1987
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3556
Gilchrist
-
Chorismate mutase from mung be ...
Sorghum bicolor, Vigna radiata
Methods Enzymol.
142
450-463
1987
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3557
Davidson
Chorismate mutase-prephenate d ...
Escherichia coli
Methods Enzymol.
142
440-450
1987
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3574
Davidson
Chorismate mutase-prephenate d ...
Cupriavidus necator, Escherichia coli, Klebsiella aerogenes, Pseudomonas sp., Salmonella enterica subsp. enterica serovar Typhimurium, Xanthomonas campestris
Methods Enzymol.
142
432-439
1987
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3552
Singh
Chorismate mutase isoenzymes f ...
Sorghum bicolor
Arch. Biochem. Biophys.
246
617-621
1986
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3553
Ball
Chorismate mutase-prephenate d ...
Saccharomyces cerevisiae
Mol. Gen. Genet.
205
326-330
1986
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3551
Singh
Chorismate mutase isoenzymes f ...
Sorghum bicolor
Arch. Biochem. Biophys.
243
374-384
1985
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3549
d'Amato
Subcellular localization of ch ...
Nicotiana sylvestris
Planta
162
104-108
1984
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3550
Goers
Separation and characterizatio ...
Nicotiana sylvestris
Planta
162
109-116
1984
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3547
Chao
Inhibition of chorismate mutas ...
Klebsiella aerogenes
Biochemistry
21
2778-2781
1982
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3548
Hoare
Chorismate mutase-catalyzed re ...
Escherichia coli, Kitasatospora aureofaciens, Kitasatospora aureofaciens tue 24
Biochem. Biophys. Res. Commun.
106
660-662
1982
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3546
Shiio
Two components of chorismate m ...
Brevibacterium flavum
J. Biochem.
86
17-25
1979
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3545
Woodin
Comparison of chorismate mutas ...
Anthophyta, Avena sativa, Dactylis glomerata, Medicago sativa, Nephrolysis sp., Pinus sp., Selaginella sp., Triticum aestivum, Vigna radiata, Zea mays
Plant Physiol.
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949-952
1978
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10
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3542
Friedrich
Purification and properties of ...
Cupriavidus necator
J. Bacteriol.
126
712-722
1976
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3543
Gething
Chorismate mutase/prephenate d ...
Escherichia coli
Eur. J. Biochem.
71
317-325
1976
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3544
Gething
Chorismate mutase/prephenate d ...
Escherichia coli
Eur. J. Biochem.
71
327-336
1976
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3541
Zurawski
Chorismate mutase of Chlamydom ...
Chlamydomonas reinhardtii
Biochim. Biophys. Acta
377
473-481
1975
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2
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3540
Görisch
Chorismate mutase from Strepto ...
Kitasatospora aureofaciens, Kitasatospora aureofaciens tue 24
Biochemistry
13
3790-3794
1974
1
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3537
Görisch
Chorismate mutase from Strepto ...
Kitasatospora aureofaciens
J. Bacteriol.
114
645-651
1973
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2
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3538
Woodin
Evidence for three isoenzymes ...
Medicago sativa
Biochim. Biophys. Acta
309
211-223
1973
2
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3539
Woodin
Chorismate mutase isozyme patt ...
Neurospora crassa, Penicillium chrysogenum, Penicillium duponti
Biochim. Biophys. Acta
309
224-231
1973
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3536
Görisch
Properties of chorismate mutas ...
Streptomyces venezuelae
Arch. Microbiol.
82
147-154
1972
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3533
Sproessler
Eigenschaften der Chorismat-Mu ...
Claviceps paspali, Claviceps sp., Claviceps sp. SD 58
Hoppe-Seyler's Z. Physiol. Chem.
351
448-459
1970
2
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4
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3534
Lorence
Multiple molecular forms of ch ...
Bacillus subtilis 23, Bacillus subtilis
Biochemistry
6
1541-1553
1967
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2
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3535
Cotton
The biosynthesis of phenylalan ...
Escherichia coli, Klebsiella aerogenes
Biochim. Biophys. Acta
100
76-88
1965
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4
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