BRENDA - Enzyme Database show
show all sequences of 1.1.1.41

Isocitrate dehydrogenase from Streptococcus mutans: biochemical properties and evaluation of a putative phosphorylation site at Ser102

Wang, P.; Song, P.; Jin, M.; Zhu, G.; PLoS ONE 8, e58918 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene idh, expression of wild-type and mutant enzymes in Escherichia coli glutamate auxotrophic strain Dicd::kanr fused to gene icd, the endogenous icd gene is replaced by the kanamycin resistance gene, the wild-type phenotype of the icd defective strain on minimal medium without glutamate is restored
Streptococcus mutans
Engineering
Amino acid exchange
Commentary
Organism
S102A
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 3.3% of wild-type activity
Streptococcus mutans
S102G
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 2.8% of wild-type activity
Streptococcus mutans
S102T
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 16% of wild-type activity
Streptococcus mutans
S102Y
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 1.1% of wild-type activity
Streptococcus mutans
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ca2+
-
Streptococcus mutans
Co2+
-
Streptococcus mutans
Cu2+
-
Streptococcus mutans
Ni2+
-
Streptococcus mutans
Zn2+
-
Streptococcus mutans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.075
-
DL-isocitrate
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
0.143
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.148
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.15
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.154
-
NAD+
pH 7.5, 37C, recombinant enzyme
Streptococcus mutans
0.246
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.295
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.35
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.385
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
1.56
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
best divalent cation
Streptococcus mutans
additional information
the enzyme is dependent on divalent cations
Streptococcus mutans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
70000
-
recombinant enzyme, gel filtration
Streptococcus mutans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
DL-isocitrate + NAD+
Streptococcus mutans
-
2-oxoglutarate + CO2 + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Streptococcus mutans
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phosphoprotein
catalytically important phosphorylation site at Ser102
Streptococcus mutans
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli
Streptococcus mutans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DL-isocitrate + NAD+
-
723607
Streptococcus mutans
2-oxoglutarate + CO2 + NADH
-
-
-
r
additional information
the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42
723607
Streptococcus mutans
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
homodimer
-
Streptococcus mutans
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
45
-
-
Streptococcus mutans
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
25
55
activity range, profile overview
Streptococcus mutans
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
40
-
purified recombinant enzyme, stable up to, rapid inactivation above
Streptococcus mutans
50
-
purified recombinant enzyme, inactivation
Streptococcus mutans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.5
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
3
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
3.3
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
3.5
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
4
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
9.1
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
25
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
56
-
NAD+
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
59
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
124
-
DL-isocitrate
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Streptococcus mutans
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.2
9.2
activity range, profile overview
Streptococcus mutans
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42
Streptococcus mutans
NAD+
-
Streptococcus mutans
NADH
-
Streptococcus mutans
Cloned(Commentary) (protein specific)
Commentary
Organism
gene idh, expression of wild-type and mutant enzymes in Escherichia coli glutamate auxotrophic strain Dicd::kanr fused to gene icd, the endogenous icd gene is replaced by the kanamycin resistance gene, the wild-type phenotype of the icd defective strain on minimal medium without glutamate is restored
Streptococcus mutans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42
Streptococcus mutans
NAD+
-
Streptococcus mutans
NADH
-
Streptococcus mutans
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
S102A
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 3.3% of wild-type activity
Streptococcus mutans
S102G
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 2.8% of wild-type activity
Streptococcus mutans
S102T
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 16% of wild-type activity
Streptococcus mutans
S102Y
site-directed mutagenesis, the mutant shows decreased affinity for isocitrate and 1.1% of wild-type activity
Streptococcus mutans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ca2+
-
Streptococcus mutans
Co2+
-
Streptococcus mutans
Cu2+
-
Streptococcus mutans
Ni2+
-
Streptococcus mutans
Zn2+
-
Streptococcus mutans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.075
-
DL-isocitrate
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
0.143
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.148
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.15
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.154
-
NAD+
pH 7.5, 37C, recombinant enzyme
Streptococcus mutans
0.246
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.295
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.35
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.385
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
1.56
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
best divalent cation
Streptococcus mutans
additional information
the enzyme is dependent on divalent cations
Streptococcus mutans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
70000
-
recombinant enzyme, gel filtration
Streptococcus mutans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
DL-isocitrate + NAD+
Streptococcus mutans
-
2-oxoglutarate + CO2 + NADH
-
-
r
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phosphoprotein
catalytically important phosphorylation site at Ser102
Streptococcus mutans
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant enzymes from Escherichia coli
Streptococcus mutans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
DL-isocitrate + NAD+
-
723607
Streptococcus mutans
2-oxoglutarate + CO2 + NADH
-
-
-
r
additional information
the enzyme is also active with NADP+ and NADPH, cf. EC 1.1.1.42
723607
Streptococcus mutans
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
-
Streptococcus mutans
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
45
-
-
Streptococcus mutans
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
25
55
activity range, profile overview
Streptococcus mutans
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
40
-
purified recombinant enzyme, stable up to, rapid inactivation above
Streptococcus mutans
50
-
purified recombinant enzyme, inactivation
Streptococcus mutans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.5
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
3
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
3.3
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
3.5
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
4
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
9.1
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
25
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
56
-
NAD+
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
59
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
124
-
DL-isocitrate
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Streptococcus mutans
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.2
9.2
activity range, profile overview
Streptococcus mutans
General Information
General Information
Commentary
Organism
evolution
the ancient NAD-dependent IDHs might be the underlying origin of phosphorylation mechanism used by their bacterial NADP-dependent homologues
Streptococcus mutans
additional information
Ser102 plays an important role in substrate binding and is required for the enzyme function
Streptococcus mutans
General Information (protein specific)
General Information
Commentary
Organism
evolution
the ancient NAD-dependent IDHs might be the underlying origin of phosphorylation mechanism used by their bacterial NADP-dependent homologues
Streptococcus mutans
additional information
Ser102 plays an important role in substrate binding and is required for the enzyme function
Streptococcus mutans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.000002
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
0.000004
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
0.00001
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.000022
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.000028
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.00003
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.00017
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.00017
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.00036
-
NAD+
pH 7.5, 37C, recombinant enzyme
Streptococcus mutans
0.00165
-
DL-isocitrate
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.000002
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
0.000004
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102Y
Streptococcus mutans
0.00001
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.000022
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102A
Streptococcus mutans
0.000028
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.00003
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102G
Streptococcus mutans
0.00017
-
DL-isocitrate
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.00017
-
NAD+
pH 7.5, 37C, recombinant enzyme mutant S102T
Streptococcus mutans
0.00036
-
NAD+
pH 7.5, 37C, recombinant enzyme
Streptococcus mutans
0.00165
-
DL-isocitrate
pH 7.5, 37C, recombinant wild-type enzyme
Streptococcus mutans
Other publictions for EC 1.1.1.41
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)
723607
Wang
Isocitrate dehydrogenase from ...
Streptococcus mutans
PLoS ONE
8
e58918
2013
-
-
1
-
4
-
5
10
-
2
1
1
-
2
-
1
1
-
-
-
-
-
2
1
1
1
2
10
1
1
-
3
-
-
-
-
-
1
3
-
4
-
-
5
-
10
-
2
1
1
-
-
1
1
-
-
-
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1
1
1
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9
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-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
2
-
-
-
-
-
-
-
4
-
-
4
-
-
-
-
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2
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-
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1
-
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1
-
7
-
-
-
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-
-
1
-
1
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
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-
-
1
-
-
-
5
4
-
4
2
2
-
4
-
-
1
-
-
-
-
-
6
1
1
1
1
4
2
1
-
2
-
-
-
-
-
1
2
-
-
-
-
5
-
4
-
4
2
2
-
-
-
1
-
-
-
-
6
1
1
1
1
4
2
1
-
-
-
1
1
-
4
4
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2
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-
4
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-
1
2
1
-
2
-
-
1
-
-
-
-
-
1
2
1
-
-
-
1
-
-
1
-
-
-
2
-
1
1
-
4
-
-
1
-
18
-
1
2
1
-
-
-
1
-
-
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-
1
2
1
-
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-
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1
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1
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7
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12
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-
2
-
-
1
-
-
-
-
-
2
1
1
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
7
-
-
-
-
12
2
1
-
1
-
-
-
1
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
713076
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-
-
1
-
1
-
-
-
2
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
713380
Zhang
Genetic analysis of central ca ...
Zea mays
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-
-
1
-
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
696358
Garcia
Disulfide bond formation in ye ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Biochemistry
48
8869-8878
2009
-
-
1
-
2
-
1
-
-
-
2
-
-
8
-
-
1
-
-
-
-
-
2
1
-
-
-
-
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1
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2
1
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712180
Kang
Mutational analysis of IDH1 co ...
Homo sapiens
Int. J. Cancer
125
353-355
2009
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1
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20
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7
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20
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2
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Lin
Suppression of metabolic defec ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Arch. Biochem. Biophys.
474
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2008
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687692
Taylor
Allosteric motions in structur ...
Saccharomyces cerevisiae
J. Biol. Chem.
283
10872-10880
2008
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-
1
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2
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1
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-
689940
Imada
Structure and quantum chemical ...
Acidithiobacillus thiooxidans
Proteins
70
63-71
2008
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-
1
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3
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1
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1
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695342
Hatzopoulos
Cloning, expression, purificat ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Acta Crystallogr. Sect. F
64
1139-1142
2008
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1
1
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139
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1
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2
1
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1
1
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4
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1
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2
1
-
-
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-
-
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700359
Hartong
Novel insights into the contri ...
Homo sapiens
Nat. Genet.
40
1230-1234
2008
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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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684749
Stokke
Biochemical characterization o ...
Methylococcus capsulatus
Arch. Microbiol.
187
361-370
2007
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1
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1
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2
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5
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1
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1
1
1
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1
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1
1
1
-
1
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685154
Bzymek
Role of alpha-Asp181, beta-Asp ...
Homo sapiens
Biochemistry
46
5391-5397
2007
1
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3
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8
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1
1
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2
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1
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1
1
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-
-
-
685719
Kanamasa
-
Isocitrate dehydrogenase and i ...
Eremothecium gossypii
Biotechnol. Bioprocess Eng.
12
92-99
2007
-
-
-
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1
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1
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1
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1
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689578
Lemaitre
NAD-dependent isocitrate dehyd ...
Arabidopsis thaliana
Plant Physiol.
144
1546-1558
2007
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1
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4
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667098
Hu
-
Crystallization and preliminar ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
F62
709
2006
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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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667332
Hu
Novel allosteric properties pr ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Arch. Biochem. Biophys.
453
207-216
2006
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1
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9
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10
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1
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4
1
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2
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12
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5
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3
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4
3
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669465
Hu
Physiological consequences of ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
J. Biol. Chem.
281
16935-16942
2006
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6
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1
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2
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1
1
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1
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1
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6
-
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1
3
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1
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2
-
1
1
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669477
Soundar
Identification of Mn2+-binding ...
Homo sapiens
J. Biol. Chem.
281
21073-21081
2006
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1
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12
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6
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2
1
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18
-
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2
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1
2
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7
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12
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3
2
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1
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6
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2
1
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-
-
18
-
-
-
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670547
Lemaitre
Expression analysis of Arabido ...
Arabidopsis thaliana
Plant Cell Physiol.
47
634-643
2006
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1
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1
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11
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10
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23
-
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1
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-
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1
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1
1
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-
-
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5
-
11
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-
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87
-
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1
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-
-
-
-
-
-
-
-
-
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-
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670847
Kalinina
Amino acid residues that deter ...
Escherichia coli
Proteins
64
1001-1009
2006
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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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1
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1
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
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660907
Miyazaki
Bifunctional isocitrate-homois ...
Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
331
341-346
2005
-
-
1
-
-
-
-
3
-
2
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-
3
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1
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1
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1
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2
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3
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1
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1
1
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3
-
2
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1
1
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1
-
2
-
-
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-
3
-
-
-
-
-
-
-
-
-
-
667647
Anderson
Analysis of interactions with ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Biochemistry
44
16776-16784
2005
1
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1
-
1
-
2
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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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1
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1
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2
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1
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670158
Watanabe
Elucidation of stability deter ...
Azotobacter vinelandii, Colwellia maris
Microbiology
151
1083-1094
2005
-
-
2
-
-
-
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4
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4
2
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5
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2
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-
-
2
-
2
2
2
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-
4
-
-
-
2
-
-
-
-
-
2
2
-
-
-
-
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-
4
-
4
2
-
-
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-
2
-
-
2
-
2
2
2
-
-
4
-
-
-
-
-
-
-
-
-
-
670544
Abiko
Localization of NAD-isocitrate ...
Oryza sativa
Plant Cell Physiol.
46
1724-1734
2005
-
-
-
-
-
-
-
-
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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1
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-
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1
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1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670805
Rodriguez-Arnedo
Complete reversal of coenzyme ...
Escherichia coli
Protein J.
24
259-266
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
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-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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654783
Morgunov
Regulation of NAD(+)-dependent ...
Yarrowia lipolytica
Biochemistry
69
1391-1398
2004
1
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-
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-
1
3
2
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1
2
2
-
3
-
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1
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-
-
4
-
2
1
1
-
-
-
1
-
-
1
1
-
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1
-
-
1
-
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1
-
3
1
2
-
1
2
2
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1
-
-
4
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
657111
Lin
Characterization of a mutation ...
Arabidopsis thaliana, Arabidopsis thaliana Landsberg
Plant Sci.
166
983-988
2004
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-
1
-
1
-
-
-
1
1
-
2
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2
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1
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-
6
2
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4
1
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-
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-
1
-
-
1
-
-
-
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-
1
1
-
1
-
-
-
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-
1
1
-
2
-
-
-
1
-
6
2
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
654843
Igamberdiev
Regulation of NAD- and NADP-de ...
Pisum sativum
Biochim. Biophys. Acta
1606
117-125
2003
1
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-
-
-
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3
2
1
1
-
1
-
2
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1
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-
1
2
1
2
-
-
-
-
-
1
-
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1
2
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1
-
-
1
-
-
-
-
3
2
2
1
1
-
1
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-
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1
-
1
2
1
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
654914
Pinheiro de Carvalho
-
Effect of metabolites of gamma ...
Pisum sativum, Zea mays
Biol. Bull.
30
236-242
2003
1
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-
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7
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1
1
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2
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2
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2
2
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2
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2
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2
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1
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2
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7
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1
1
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2
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2
2
-
2
-
2
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656118
Lin
Homologous binding sites in ye ...
Saccharomyces cerevisiae
J. Biol. Chem.
278
12864-12872
2003
1
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1
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4
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1
1
1
1
1
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1
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2
1
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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4
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1
1
1
1
1
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1
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-
-
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2
1
1
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1
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656189
Soundar
Evaluation by mutagenesis of t ...
Homo sapiens
J. Biol. Chem.
278
52146-52153
2003
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1
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3
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1
1
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3
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1
1
1
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1
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-
1
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-
-
1
-
1
1
-
3
-
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-
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11
-
1
1
1
-
-
-
1
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3
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1
1
1
-
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-
1
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-
-
-
-
-
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654652
Anderson
Effect of AMP on mRNA binding ...
Saccharomyces cerevisiae
Biochemistry
41
7065-7073
2002
1
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-
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1
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2
1
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2
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2
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3
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1
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1
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1
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1
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1
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2
1
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2
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-
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-
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3
-
-
-
-
-
1
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-
-
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655607
Inoue
Biochemical and molecular char ...
Acidithiobacillus thiooxidans, Acidithiobacillus thiooxidans ON107
FEMS Microbiol. Lett.
214
127-132
2002
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1
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1
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2
1
1
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2
2
1
1
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2
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-
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1
2
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-
-
-
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-
3
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1
2
2
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1
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1
-
2
1
1
-
2
2
1
1
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-
656052
Lin
Isocitrate binding at two func ...
Saccharomyces cerevisiae
J. Biol. Chem.
277
22475-22483
2002
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1
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6
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1
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1
2
2
1
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1
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1
-
-
-
1
-
1
1
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6
-
-
-
-
1
-
1
-
1
-
-
-
1
-
-
-
1
2
2
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Identification of cofactor dis ...
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Comparison of isocitrate dehyd ...
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Anderson
Allosteric inhibition of NAD+- ...
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286769
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Purification and characterizat ...
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286774
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286775
Huang
Identification of the subunits ...
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286776
Alvarez-Villafane
Two NAD+-dependent isocitrate ...
Phycomyces blakesleeanus
Biochemistry
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1996
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286777
Hurley
Determinants of cofactor speci ...
Escherichia coli
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4
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663920
Mitchell
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Identification of a multienzym ...
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286770
Gabriel
Kinetic regulation of yeast NA ...
Saccharomyces cerevisiae
Biochemistry
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1991
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16
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286767
Rutter
Regulation of NAD+-linked isoc ...
Rattus norvegicus
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286764
Gabriel
Inhibition and activation of b ...
Bos taurus
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286765
Gabriel
NAD-specific isocitrate dehydr ...
Bos taurus
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286766
Evans
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The role of the mitochondrial ...
Rhodotorula toruloides
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6
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286762
Gabriel
Inhibition of bovine heart NAD ...
Bos taurus
Biochemistry
23
2773-2778
1984
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2
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286763
Bulos
Calcium inhibition of the NAD+ ...
Phormia regina
J. Biol. Chem.
259
10232-10237
1984
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2
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286768
Gabriel
Citrate activation of NAD-spec ...
Bos taurus
J. Biol. Chem.
259
1622-1628
1984
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286761
Tezuka
Isolation and characterization ...
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286758
Willson
The activation of ox-brain NAD ...
Bos taurus
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1981
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286759
Ehrlich
Re-evaluation of molecular wei ...
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286760
Gabriel
Specific site inhibitors of NA ...
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Hoffmann
Regulation of NAD+- and NADP+- ...
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399-404
1980
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286757
Willson
The effect of pH on the allost ...
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Eur. J. Biochem.
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411-416
1980
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286755
Ramachandran
Evidence for the presence of t ...
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Proc. Natl. Acad. Sci. USA
75
252-255
1978
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286754
Nabeshima
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Partial purification and some ...
Candida tropicalis
Agric. Biol. Chem.
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509-516
1977
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1
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1
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286753
Alp
Activities of citrate synthase ...
Lepas anatifera, Locusta sp., Oryctes rhinoceros, Ovis aries, Periplaneta americana, Sarcophaga barbata, waterbug
Biochem. J.
154
689-700
1976
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Cohen
Role of manganous ion in the k ...
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286752
Silinski
The kinetics of NAD-linked iso ...
Bos taurus
Biochim. Biophys. Acta
370
1-25
1974
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Glaeser
NADP- und NAD-spezifische dehy ...
Cupriavidus necator
Arch. Microbiol.
86
327-337
1972
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-
-
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5
2
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1
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2
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1
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1
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1
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1
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1
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1
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5
-
2
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1
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1
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1
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1
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1
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286749
Plaut
-
Isocitrate dehydrogenase ...
Aspergillus niger, Bos taurus, Cavia porcellus, Columba livia, Homo sapiens, Pisum sativum, Rattus norvegicus, Saccharomyces cerevisiae
The Enzymes, 2nd Ed. (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
105-126
1963
1
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7
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3
2
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8
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1
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8
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10
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8
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7
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3
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