BRENDA - Enzyme Database show
show all sequences of 4.2.1.9

Characterization of recombinantly expressed dihydroxy-acid dehydratase from Sulfobus solfataricus - a key enzyme for the conversion of carbohydrates into chemicals

Carsten, J.M.; Philipp, A.; Sieber, V.; J. Biotechnol. 211, 31-41 (2015)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
increases activity up to 3fold. Activation modulates thermotolerance at 50C
Saccharolobus solfataricus
additional information
heat activation: the heat treatment step in purification at 80C increases the total activity about 2.5 to 3-fold and the specific activity about 20 to 30-fold
Saccharolobus solfataricus
Application
Application
Commentary
Organism
synthesis
the enzyme can be used for a convenient one-step synthesis route from D-gluconate to 2-dehydro-3-deoxy-D-gluconate
Saccharolobus solfataricus
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli BL21 (DE3)
Saccharolobus solfataricus
Inhibitors
Inhibitors
Commentary
Organism
Structure
(NH4)2Fe(SO4)2
10 mM, 50C, 45% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
BaCl2
100 mM, 50C, 43% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
butanol
-
Saccharolobus solfataricus
CaCl2
10 mM, 50C, 77% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
CuSO4
10 mM, 50C, 86% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
D-glycerate
competitive. Presence of 20 mM D-glycerate decreases catalytic activity towards D-gluconate drastically to 5% residual activity
Saccharolobus solfataricus
ethanol
-
Saccharolobus solfataricus
imidazole
leads to a complete elimination of enzyme activity towards D-gluconate
Saccharolobus solfataricus
isobutanol
-
Saccharolobus solfataricus
ZnCl2
10 mM, 50C, 95% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1
-
2,3-Dihydroxy-3-methylbutanoate
pH 7, 50C
Saccharolobus solfataricus
7.8
-
D-gluconate
pH 7, 50C
Saccharolobus solfataricus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe-S center
-
Saccharolobus solfataricus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2,3-dihydroxy-3-methylbutanoate
Saccharolobus solfataricus
biosynthesis pathway of the branched chain amino acids valine and isoleucine
3-methyl-2-oxobutanoate + H2O
-
-
?
2,3-dihydroxy-3-methylbutanoate
Saccharolobus solfataricus P2
biosynthesis pathway of the branched chain amino acids valine and isoleucine
3-methyl-2-oxobutanoate + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharolobus solfataricus
Q97UB2
-
-
Saccharolobus solfataricus P2
Q97UB2
-
-
Purification (Commentary)
Commentary
Organism
-
Saccharolobus solfataricus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
10.7
-
pH 7, 50C, conversion of D-glycerate to pyruvate
Saccharolobus solfataricus
Storage Stability
Storage Stability
Organism
-80C, after purification of His-tagged enzyme the total enzyme activity is decreased to 43% of the crude extract and even further to 17% when stored at -80 C for one day
Saccharolobus solfataricus
-80C, specific activity for D-gluconate of the frozen/thawed enzyme is stable for 60 min, but loses about 70% after a maximum of 100 min
Saccharolobus solfataricus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-dihydroxy-3-methylbutanoate
-
732214
Saccharolobus solfataricus
3-methyl-2-oxobutanoate + H2O
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
biosynthesis pathway of the branched chain amino acids valine and isoleucine
732214
Saccharolobus solfataricus
3-methyl-2-oxobutanoate + H2O
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
-
732214
Saccharolobus solfataricus P2
3-methyl-2-oxobutanoate + H2O
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
biosynthesis pathway of the branched chain amino acids valine and isoleucine
732214
Saccharolobus solfataricus P2
3-methyl-2-oxobutanoate + H2O
-
-
-
?
D-gluconate
-
732214
Saccharolobus solfataricus
2-dehydro-3-deoxy-D-gluconate + H2O
-
-
-
?
D-gluconate
-
732214
Saccharolobus solfataricus P2
2-dehydro-3-deoxy-D-gluconate + H2O
-
-
-
?
D-glycerate
the enzyme catalyzes the non-natural dehydration of D-glycerate to pyruvate
732214
Saccharolobus solfataricus
pyruvate + H2O
-
-
-
?
D-glycerate
the enzyme catalyzes the non-natural dehydration of D-glycerate to pyruvate
732214
Saccharolobus solfataricus P2
pyruvate + H2O
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
77
-
dehydration of D-gluconate
Saccharolobus solfataricus
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
50
-
half-life: 1028 min
Saccharolobus solfataricus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.011
-
D-glycerate
pH 7, 50C, non-activated enzyme
Saccharolobus solfataricus
0.03
-
D-glycerate
pH 7, 50C, enzyme activated by 2-mercaptoethanol
Saccharolobus solfataricus
0.31
-
2,3-Dihydroxy-3-methylbutanoate
pH 7, 50C, enzyme activated by 2-mercaptoethanol; pH 7, 50C, non-activated enzyme
Saccharolobus solfataricus
0.4
-
D-gluconate
pH 7, 50C, non-activated enzyme
Saccharolobus solfataricus
1.19
-
D-gluconate
pH 7, 50C, enzyme activated by 2-mercaptoethanol
Saccharolobus solfataricus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
-
dehydration of D-gluconate
Saccharolobus solfataricus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.2
8.2
pH 5.2: about 40% of maximal activity, pH 8.2: about 40% of maximal activity, dehydration of D-gluconate
Saccharolobus solfataricus
Cofactor
Cofactor
Commentary
Organism
Structure
Fe-S center
-
Saccharolobus solfataricus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.3
-
D-glycerate
50C, pH 7
Saccharolobus solfataricus
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
additional information
-
IC50: 4.5% (v/v)
Saccharolobus solfataricus
butanol
additional information
-
IC50: 15% (v/v)
Saccharolobus solfataricus
ethanol
additional information
-
IC50: 4% (v/v)
Saccharolobus solfataricus
isobutanol
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
2-mercaptoethanol
increases activity up to 3fold. Activation modulates thermotolerance at 50C
Saccharolobus solfataricus
additional information
heat activation: the heat treatment step in purification at 80C increases the total activity about 2.5 to 3-fold and the specific activity about 20 to 30-fold
Saccharolobus solfataricus
Application (protein specific)
Application
Commentary
Organism
synthesis
the enzyme can be used for a convenient one-step synthesis route from D-gluconate to 2-dehydro-3-deoxy-D-gluconate
Saccharolobus solfataricus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli BL21 (DE3)
Saccharolobus solfataricus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Fe-S center
-
Saccharolobus solfataricus
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
additional information
-
IC50: 4.5% (v/v)
Saccharolobus solfataricus
butanol
additional information
-
IC50: 15% (v/v)
Saccharolobus solfataricus
ethanol
additional information
-
IC50: 4% (v/v)
Saccharolobus solfataricus
isobutanol
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(NH4)2Fe(SO4)2
10 mM, 50C, 45% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
BaCl2
100 mM, 50C, 43% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
butanol
-
Saccharolobus solfataricus
CaCl2
10 mM, 50C, 77% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
CuSO4
10 mM, 50C, 86% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
D-glycerate
competitive. Presence of 20 mM D-glycerate decreases catalytic activity towards D-gluconate drastically to 5% residual activity
Saccharolobus solfataricus
ethanol
-
Saccharolobus solfataricus
imidazole
leads to a complete elimination of enzyme activity towards D-gluconate
Saccharolobus solfataricus
isobutanol
-
Saccharolobus solfataricus
ZnCl2
10 mM, 50C, 95% loss of activity, dehydration of D-gluconate
Saccharolobus solfataricus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
2.3
-
D-glycerate
50C, pH 7
Saccharolobus solfataricus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
2.1
-
2,3-Dihydroxy-3-methylbutanoate
pH 7, 50C
Saccharolobus solfataricus
7.8
-
D-gluconate
pH 7, 50C
Saccharolobus solfataricus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe-S center
-
Saccharolobus solfataricus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2,3-dihydroxy-3-methylbutanoate
Saccharolobus solfataricus
biosynthesis pathway of the branched chain amino acids valine and isoleucine
3-methyl-2-oxobutanoate + H2O
-
-
?
2,3-dihydroxy-3-methylbutanoate
Saccharolobus solfataricus P2
biosynthesis pathway of the branched chain amino acids valine and isoleucine
3-methyl-2-oxobutanoate + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharolobus solfataricus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
10.7
-
pH 7, 50C, conversion of D-glycerate to pyruvate
Saccharolobus solfataricus
Storage Stability (protein specific)
Storage Stability
Organism
-80C, after purification of His-tagged enzyme the total enzyme activity is decreased to 43% of the crude extract and even further to 17% when stored at -80 C for one day
Saccharolobus solfataricus
-80C, specific activity for D-gluconate of the frozen/thawed enzyme is stable for 60 min, but loses about 70% after a maximum of 100 min
Saccharolobus solfataricus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-dihydroxy-3-methylbutanoate
-
732214
Saccharolobus solfataricus
3-methyl-2-oxobutanoate + H2O
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
biosynthesis pathway of the branched chain amino acids valine and isoleucine
732214
Saccharolobus solfataricus
3-methyl-2-oxobutanoate + H2O
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
-
732214
Saccharolobus solfataricus P2
3-methyl-2-oxobutanoate + H2O
-
-
-
?
2,3-dihydroxy-3-methylbutanoate
biosynthesis pathway of the branched chain amino acids valine and isoleucine
732214
Saccharolobus solfataricus P2
3-methyl-2-oxobutanoate + H2O
-
-
-
?
D-gluconate
-
732214
Saccharolobus solfataricus
2-dehydro-3-deoxy-D-gluconate + H2O
-
-
-
?
D-gluconate
-
732214
Saccharolobus solfataricus P2
2-dehydro-3-deoxy-D-gluconate + H2O
-
-
-
?
D-glycerate
the enzyme catalyzes the non-natural dehydration of D-glycerate to pyruvate
732214
Saccharolobus solfataricus
pyruvate + H2O
-
-
-
?
D-glycerate
the enzyme catalyzes the non-natural dehydration of D-glycerate to pyruvate
732214
Saccharolobus solfataricus P2
pyruvate + H2O
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
77
-
dehydration of D-gluconate
Saccharolobus solfataricus
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
50
-
half-life: 1028 min
Saccharolobus solfataricus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.011
-
D-glycerate
pH 7, 50C, non-activated enzyme
Saccharolobus solfataricus
0.03
-
D-glycerate
pH 7, 50C, enzyme activated by 2-mercaptoethanol
Saccharolobus solfataricus
0.31
-
2,3-Dihydroxy-3-methylbutanoate
pH 7, 50C, enzyme activated by 2-mercaptoethanol; pH 7, 50C, non-activated enzyme
Saccharolobus solfataricus
0.4
-
D-gluconate
pH 7, 50C, non-activated enzyme
Saccharolobus solfataricus
1.19
-
D-gluconate
pH 7, 50C, enzyme activated by 2-mercaptoethanol
Saccharolobus solfataricus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.2
-
dehydration of D-gluconate
Saccharolobus solfataricus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.2
8.2
pH 5.2: about 40% of maximal activity, pH 8.2: about 40% of maximal activity, dehydration of D-gluconate
Saccharolobus solfataricus
General Information
General Information
Commentary
Organism
metabolism
biosynthesis pathway of the branched chain amino acids valine and isoleucine
Saccharolobus solfataricus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
biosynthesis pathway of the branched chain amino acids valine and isoleucine
Saccharolobus solfataricus
Other publictions for EC 4.2.1.9
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)
748233
Gao
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3
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1
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732214
Carsten
Characterization of recombinan ...
Saccharolobus solfataricus, Saccharolobus solfataricus P2
J. Biotechnol.
211
31-41
2015
2
1
1
-
-
-
10
2
-
1
-
2
-
5
-
-
1
-
-
-
1
2
8
-
1
-
1
5
1
1
-
1
1
-
3
2
1
1
1
-
-
-
3
10
1
2
-
1
-
2
-
-
-
1
-
-
1
2
8
-
1
-
1
5
1
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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2
2
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1
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1
-
1
-
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748324
Zhang
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Arabidopsis thaliana
J. Exp. Bot.
66
879-888
2015
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7
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2
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2
-
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-
-
-
1
1
-
-
-
730702
Oliver
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Aspergillus fumigatus
PLoS ONE
7
e43559
2012
-
-
1
-
-
-
1
1
1
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1
-
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7
-
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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
1
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1
1
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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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713917
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91
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1
-
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-
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1
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3
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1
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1
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1
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1
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-
-
-
-
-
-
-
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-
714551
Park
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Escherichia coli
Biotechnol. Bioeng.
108
1140-1147
2011
-
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1
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-
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-
-
-
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4
-
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1
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716148
Singh
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Escherichia coli, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Microbiology
157
38-46
2011
-
1
1
-
1
-
1
1
-
1
2
-
-
157
-
-
1
-
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1
1
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2
1
-
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1
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1
1
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1
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1
-
1
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Bacteriostatic effect of 4,7-d ...
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33980
Matsumura
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Isolation and characterization ...
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Xing
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Pirrung
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Flint
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An activity stain for dihydrox ...
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33984
Smyk-Randall
A reverse-phase high-performan ...
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33974
Armstrong
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Structure-activity studies wit ...
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1985
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33971
Brown
Dihydroxyacid dehydratase: the ...
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33970
Armstrong
Stereoselectivity and stereosp ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochim. Biophys. Acta
498
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1977
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33968
Armstrong
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Stereochemistry of the reducto ...
Salmonella enterica subsp. enterica serovar Typhimurium
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33969
Ryan
Subcellular localization of is ...
Saccharomyces cerevisiae
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1974
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Cassady
Separation of mitochondrial me ...
Neurospora crassa
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66-72
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33966
Twarog
Enzymes of the isoleucine-vali ...
Acinetobacter sp. 15150, Acinetobacter sp.
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37-46
1972
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33967
Altmiller
Neurospora mutants with mitoch ...
Neurospora crassa
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1972
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2
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33962
Wixom
A rapid determination of dihyd ...
Escherichia coli, Klebsiella aerogenes
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262-274
1971
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33964
Wixom
Studies in valine biosynthesis ...
Achromobacter ruhlandii, Acidovorax facilis, Chromatium sp., Chromatium sp. D, Cupriavidus necator, Paracoccus denitrificans, Rhodobacter sphaeroides, Rhodospirillum rubrum
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2
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16
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1
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2
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1
-
-
1
1
-
2
-
-
-
5
-
2
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
1
-
-
-
-
-
-
1
-
1
1
-
2
-
-
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5
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2
2
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-
-
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4
2
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4
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2
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2
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-
-
2
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4
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-
-
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3
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-
-
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4
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2
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4
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2
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2
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4
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-
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3
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8
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2
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2
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1
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1
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4
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1
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1
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8
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2
2
3
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2
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1
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1
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4
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1
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1
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1
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1
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4
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2
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4
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3
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2
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1
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1
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4
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2
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