BRENDA - Enzyme Database
show all sequences of 1.1.1.41

Novel type II and monomeric NAD+ specific isocitrate dehydrogenases: phylogenetic affinity, enzymatic characterization, and evolutionary implication

Wang, P.; Lv, C.; Zhu, G.; Sci. Rep. 5, 9150 (2015)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene HMPREF1139_0890, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant His6-tagged enzymes in Escherichia coli
Campylobacter sp.
gene icd, sequence comparisons and phylogenetic analysis
Campylobacter curvus
gene icd, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant His6-tagged enzymes in Escherichia coli
Ostreococcus sp. 'lucimarinus'
gene IDHP, sequence comparisons and phylogenetic analysis
Micromonas commoda
Engineering
Amino acid exchange
Commentary
Organism
D326R/M327H
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH Asp326/Met327 is completely reversed from NAD+ to NADP+
Ostreococcus sp. 'lucimarinus'
D326X/M327X
site-directed mutagenesis, the coenzyme specificity of the mutant OlIDH R326H327 is completely reversed from NAD+ to NADP+
Ostreococcus sp. 'lucimarinus'
L584H/D595R
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH H584/R595 is completely reversed from NAD+ to NADP+
Campylobacter sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
Ca2+
complete inhibition at 2 mM
Campylobacter sp.
Cu2+
complete inhibition at 2 mM
Campylobacter sp.
Cu2+
complete inhibition at 2 mM
Ostreococcus sp. 'lucimarinus'
Zn2+
complete inhibition at 2 mM
Campylobacter sp.
Zn2+
complete inhibition at 2 mM
Ostreococcus sp. 'lucimarinus'
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0082
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
0.0114
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
0.0289
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
0.0742
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
0.126
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
0.136
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
0.476
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
0.493
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
0.513
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
1.827
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
2.211
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
2.948
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates, 13.6% activity compared to Mg2+ for OlIDH
Ostreococcus sp. 'lucimarinus'
Co2+
activates, 35.5% activity compared to Mg2+ for CaIDH
Campylobacter sp.
Mg2+
activates, 78.3% activity compared to Mg2+ for CaIDH
Campylobacter sp.
Mg2+
activates, 68.6% activity compared to Mg2+ for OlIDH
Ostreococcus sp. 'lucimarinus'
Mn2+
activates, Mn2+ is the most favorable cation for CaIDH
Campylobacter sp.
Mn2+
activates, Mn2+ is the most favorable cation for OlIDH
Ostreococcus sp. 'lucimarinus'
additional information
divalent cations are required for activity
Campylobacter curvus
additional information
divalent cations are required for activity, low or poor activation by Rb+, Ni2+, K+, Na+, and Li+
Campylobacter sp.
additional information
divalent cations are required for activity
Micromonas commoda
additional information
divalent cations are required for activity, low or poor activation by Co2+, Ni2+, K+, Na+, and Li+
Ostreococcus sp. 'lucimarinus'
Rb+
activates, 11.0% activity compared to Mg2+ for OlIDH
Ostreococcus sp. 'lucimarinus'
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
-
Ostreococcus sp. 'lucimarinus'
80000
-
-
Campylobacter sp.
81000
-
recombinant His6-tagged enzyme, gel filtration
Campylobacter sp.
92000
-
recombinant His6-tagged enzyme, gel filtration
Ostreococcus sp. 'lucimarinus'
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
isocitrate + NAD+
Ostreococcus sp. 'lucimarinus'
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Micromonas commoda
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter sp.
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter curvus
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Ostreococcus sp. 'lucimarinus' CCE9901
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter curvus 525.92
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter sp. FOBRC14
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Micromonas commoda RCC299
-
2-oxoglutarate + CO2 + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Campylobacter curvus
A0A0M4S9Q1
-
-
Campylobacter curvus 525.92
A0A0M4S9Q1
-
-
Campylobacter sp.
J4X756
-
-
Campylobacter sp. FOBRC14
J4X756
-
-
Micromonas commoda
C1E5X2
-
-
Micromonas commoda RCC299
C1E5X2
-
-
Ostreococcus sp. 'lucimarinus'
A4SBK5
-
-
Ostreococcus sp. 'lucimarinus'
-
-
-
Ostreococcus sp. 'lucimarinus' CCE9901
A4SBK5
-
-
Ostreococcus sp. 'lucimarinus' CCE9901
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant His6-tagged enzymes from Escherichia coli
Campylobacter sp.
recombinant wild-type and mutant His6-tagged enzymes from Escherichia coli
Ostreococcus sp. 'lucimarinus'
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.8
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NADP+
Ostreococcus sp. 'lucimarinus'
8.7
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NADP+
Campylobacter sp.
53.2
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NAD+
Campylobacter sp.
72.3
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NAD+
Ostreococcus sp. 'lucimarinus'
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
isocitrate + NAD+
-
741414
Ostreococcus sp. 'lucimarinus'
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Micromonas commoda
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter sp.
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter curvus
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Ostreococcus sp. 'lucimarinus' CCE9901
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter curvus 525.92
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter sp. FOBRC14
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Micromonas commoda RCC299
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Micromonas commoda
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter sp.
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter curvus
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Ostreococcus sp. 'lucimarinus'
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Ostreococcus sp. 'lucimarinus' CCE9901
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter curvus 525.92
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter sp. FOBRC14
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Micromonas commoda RCC299
2-oxoglutarate + CO2 + NADPH
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
-
Micromonas commoda
homodimer
; 2 * 45000, recombinant His6-tagged enzyme, SDS-PAGE
Ostreococcus sp. 'lucimarinus'
monomer
-
Campylobacter curvus
monomer
1 * 80000, recombinant His6-tagged enzyme, SDS-PAGE
Campylobacter sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Campylobacter curvus
25
-
assay at
Micromonas commoda
40
-
with Mn2+
Campylobacter sp.
40
-
with Mg2+ or Mn2+
Ostreococcus sp. 'lucimarinus'
45
-
with Mg2+
Campylobacter sp.
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
55
recombinant CaIDH retains the majority of the activity below 45°C, its activity drops rapidly as the temperature is raised. Incubation at 55°C for 20 min causes a 55% or 75% loss of activity in the presence of Mg2+ or Mn2+, respectively
Campylobacter sp.
45
50
recombinant OlIDH is stable below 45°C, but its activity rapidly declines as the temperature is raised. Incubation at 45°C for 20 min causes a 28% or 21% loss of activity in the presence of Mg2+ or Mn2+, respectively, whereas incubation at 50°C causes a 91% or 84% loss of activity in the presence of Mg2+ or Mn2+, respectively
Ostreococcus sp. 'lucimarinus'
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.4
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
1.8
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
1.9
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
2
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
4.2
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
7
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
9.5
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
10
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
10.8
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
22.5
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
29.1
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
60.6
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Campylobacter curvus
7.5
-
with Mn2+
Campylobacter sp.
7.5
-
assay at
Micromonas commoda
8
-
with Mg2+
Campylobacter sp.
8.5
-
with Mn2+
Ostreococcus sp. 'lucimarinus'
9
-
with Mg2+
Ostreococcus sp. 'lucimarinus'
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
specific for, the enzyme displays 37fold preference for NAD+ over NADP+
Campylobacter curvus
NAD+
specific for, the enzyme displays 61fold preference for NAD+ over NADP+. Putative coenzyme discriminating amino acids residues are Leu584 and Asp595 in CaIDH
Campylobacter sp.
NAD+
specific for, the enzyme displays 224fold preference for NAD+ over NADP+
Micromonas commoda
NAD+
specific for, the enzyme displays 99fold preference for NAD+ over NADP+; specific for, the enzyme displays 99fold preference for NAD+ over NADP+. Putative coenzyme discriminating amino acids residues are Asp326 and Met327 in OlIDH
Ostreococcus sp. 'lucimarinus'
Cloned(Commentary) (protein specific)
Commentary
Organism
gene HMPREF1139_0890, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant His6-tagged enzymes in Escherichia coli
Campylobacter sp.
gene icd, sequence comparisons and phylogenetic analysis
Campylobacter curvus
gene icd, sequence comparisons and phylogenetic analysis, recombinant overexpression of wild-type and mutant His6-tagged enzymes in Escherichia coli
Ostreococcus sp. 'lucimarinus'
gene IDHP, sequence comparisons and phylogenetic analysis
Micromonas commoda
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
specific for, the enzyme displays 37fold preference for NAD+ over NADP+
Campylobacter curvus
NAD+
specific for, the enzyme displays 61fold preference for NAD+ over NADP+. Putative coenzyme discriminating amino acids residues are Leu584 and Asp595 in CaIDH
Campylobacter sp.
NAD+
specific for, the enzyme displays 224fold preference for NAD+ over NADP+
Micromonas commoda
NAD+
specific for, the enzyme displays 99fold preference for NAD+ over NADP+. Putative coenzyme discriminating amino acids residues are Asp326 and Met327 in OlIDH
Ostreococcus sp. 'lucimarinus'
NAD+
specific for, the enzyme displays 99fold preference for NAD+ over NADP+
Ostreococcus sp. 'lucimarinus'
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D326R/M327H
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH Asp326/Met327 is completely reversed from NAD+ to NADP+
Ostreococcus sp. 'lucimarinus'
D326X/M327X
site-directed mutagenesis, the coenzyme specificity of the mutant OlIDH R326H327 is completely reversed from NAD+ to NADP+
Ostreococcus sp. 'lucimarinus'
L584H/D595R
site-directed mutagenesis, the coenzyme specificity of the mutant CaIDH H584/R595 is completely reversed from NAD+ to NADP+
Campylobacter sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Ca2+
complete inhibition at 2 mM
Campylobacter sp.
Cu2+
complete inhibition at 2 mM
Campylobacter sp.
Cu2+
complete inhibition at 2 mM
Ostreococcus sp. 'lucimarinus'
Zn2+
complete inhibition at 2 mM
Campylobacter sp.
Zn2+
complete inhibition at 2 mM
Ostreococcus sp. 'lucimarinus'
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0082
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
0.0114
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
0.0289
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
0.0742
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
0.126
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
0.136
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
0.476
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
0.493
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
0.513
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
1.827
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
2.211
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
2.948
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates, 13.6% activity compared to Mg2+ for OlIDH
Ostreococcus sp. 'lucimarinus'
Co2+
activates, 35.5% activity compared to Mg2+ for CaIDH
Campylobacter sp.
Mg2+
activates, 78.3% activity compared to Mg2+ for CaIDH
Campylobacter sp.
Mg2+
activates, 68.6% activity compared to Mg2+ for OlIDH
Ostreococcus sp. 'lucimarinus'
Mn2+
activates, Mn2+ is the most favorable cation for CaIDH
Campylobacter sp.
Mn2+
activates, Mn2+ is the most favorable cation for OlIDH
Ostreococcus sp. 'lucimarinus'
additional information
divalent cations are required for activity
Campylobacter curvus
additional information
divalent cations are required for activity, low or poor activation by Rb+, Ni2+, K+, Na+, and Li+
Campylobacter sp.
additional information
divalent cations are required for activity
Micromonas commoda
additional information
divalent cations are required for activity, low or poor activation by Co2+, Ni2+, K+, Na+, and Li+
Ostreococcus sp. 'lucimarinus'
Rb+
activates, 11.0% activity compared to Mg2+ for OlIDH
Ostreococcus sp. 'lucimarinus'
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
45000
-
-
Ostreococcus sp. 'lucimarinus'
80000
-
-
Campylobacter sp.
81000
-
recombinant His6-tagged enzyme, gel filtration
Campylobacter sp.
92000
-
recombinant His6-tagged enzyme, gel filtration
Ostreococcus sp. 'lucimarinus'
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
isocitrate + NAD+
Ostreococcus sp. 'lucimarinus'
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Micromonas commoda
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter sp.
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter curvus
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Ostreococcus sp. 'lucimarinus' CCE9901
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter curvus 525.92
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Campylobacter sp. FOBRC14
-
2-oxoglutarate + CO2 + NADH
-
-
?
isocitrate + NAD+
Micromonas commoda RCC299
-
2-oxoglutarate + CO2 + NADH
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant His6-tagged enzymes from Escherichia coli
Campylobacter sp.
recombinant wild-type and mutant His6-tagged enzymes from Escherichia coli
Ostreococcus sp. 'lucimarinus'
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.8
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NADP+
Ostreococcus sp. 'lucimarinus'
8.7
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NADP+
Campylobacter sp.
53.2
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NAD+
Campylobacter sp.
72.3
-
purified recombinant His6-tagged enzyme, pH 7.5, 25°C, with NAD+
Ostreococcus sp. 'lucimarinus'
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
isocitrate + NAD+
-
741414
Ostreococcus sp. 'lucimarinus'
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Micromonas commoda
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter sp.
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter curvus
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Ostreococcus sp. 'lucimarinus' CCE9901
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter curvus 525.92
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Campylobacter sp. FOBRC14
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NAD+
-
741414
Micromonas commoda RCC299
2-oxoglutarate + CO2 + NADH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Micromonas commoda
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter sp.
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter curvus
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Ostreococcus sp. 'lucimarinus'
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Ostreococcus sp. 'lucimarinus' CCE9901
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter curvus 525.92
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Campylobacter sp. FOBRC14
2-oxoglutarate + CO2 + NADPH
-
-
-
?
isocitrate + NADP+
very low activity
741414
Micromonas commoda RCC299
2-oxoglutarate + CO2 + NADPH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
-
Micromonas commoda
homodimer
-
Ostreococcus sp. 'lucimarinus'
homodimer
2 * 45000, recombinant His6-tagged enzyme, SDS-PAGE
Ostreococcus sp. 'lucimarinus'
monomer
-
Campylobacter curvus
monomer
1 * 80000, recombinant His6-tagged enzyme, SDS-PAGE
Campylobacter sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Campylobacter curvus
25
-
assay at
Micromonas commoda
40
-
with Mn2+
Campylobacter sp.
40
-
with Mg2+ or Mn2+
Ostreococcus sp. 'lucimarinus'
45
-
with Mg2+
Campylobacter sp.
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
40
55
recombinant CaIDH retains the majority of the activity below 45°C, its activity drops rapidly as the temperature is raised. Incubation at 55°C for 20 min causes a 55% or 75% loss of activity in the presence of Mg2+ or Mn2+, respectively
Campylobacter sp.
45
50
recombinant OlIDH is stable below 45°C, but its activity rapidly declines as the temperature is raised. Incubation at 45°C for 20 min causes a 28% or 21% loss of activity in the presence of Mg2+ or Mn2+, respectively, whereas incubation at 50°C causes a 91% or 84% loss of activity in the presence of Mg2+ or Mn2+, respectively
Ostreococcus sp. 'lucimarinus'
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.4
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
1.8
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
1.9
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
2
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
4.2
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
7
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
9.5
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
10
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
10.8
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
22.5
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
29.1
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
60.6
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Campylobacter curvus
7.5
-
with Mn2+
Campylobacter sp.
7.5
-
assay at
Micromonas commoda
8
-
with Mg2+
Campylobacter sp.
8.5
-
with Mn2+
Ostreococcus sp. 'lucimarinus'
9
-
with Mg2+
Ostreococcus sp. 'lucimarinus'
General Information
General Information
Commentary
Organism
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
Campylobacter curvus
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
Campylobacter sp.
evolution
evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes
Micromonas commoda
evolution
evolutionary relationships of IDHs, overview; evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and is clustered into a unique clade among the type II subfamily
Ostreococcus sp. 'lucimarinus'
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Campylobacter curvus
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Campylobacter sp.
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Micromonas commoda
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Ostreococcus sp. 'lucimarinus'
General Information (protein specific)
General Information
Commentary
Organism
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
Campylobacter curvus
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes
Campylobacter sp.
evolution
evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes
Micromonas commoda
evolution
evolutionary relationships of IDHs, overview
Ostreococcus sp. 'lucimarinus'
evolution
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and is clustered into a unique clade among the type II subfamily
Ostreococcus sp. 'lucimarinus'
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Campylobacter curvus
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Campylobacter sp.
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Micromonas commoda
metabolism
NAD-IDH is a key enzyme in the tricarboxylic acid cycle. It catalyzes the oxidative decarboxylation of isocitrate to 2-oxoglutarate and CO2, which is accompanied by the reduction of NAD+ to NADH. The IDH reaction provides organisms with not only energy but also biosynthetic precursors, such as 2-oxoglutarate, for metabolism
Ostreococcus sp. 'lucimarinus'
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.8
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
4
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
4
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
4.5
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
10
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
19.3
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
146
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
179
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
220
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
242
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
368
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
444
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.8
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
4
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
4
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
4.5
-
NADP+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
10
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
19.3
-
NAD+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
146
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter curvus
179
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Micromonas commoda
220
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant D326R/M327H
Ostreococcus sp. 'lucimarinus'
242
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Campylobacter sp.
368
-
NADP+
pH 75, 25°C, recombinant His6-tagged mutant L584H/D595R
Campylobacter sp.
444
-
NAD+
pH 75, 25°C, recombinant His6-tagged enzyme
Ostreococcus sp. 'lucimarinus'
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)
740114
Hagras
Mobile phones electromagnetic ...
Homo sapiens
Biochimie Open
3
19-25
2016
-
1
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
1
-
-
1
1
1
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
1
1
-
-
-
-
-
-
-
-
2
2
-
-
-
740425
Tang
A unique homodimeric NAD+-link ...
Ostreococcus tauri
FASEB J.
29
2462-2472
2015
-
-
1
-
3
-
4
9
2
2
3
1
-
3
-
-
1
-
-
-
-
-
3
2
-
-
-
8
1
-
-
2
1
-
-
-
-
1
2
-
3
-
-
4
1
9
2
2
3
1
-
-
-
1
-
-
-
-
3
2
-
-
-
8
1
-
-
-
-
3
3
-
8
8
741236
Wu
A novel type II NAD+-specific ...
Congregibacter litoralis, Congregibacter litoralis KT71
PLoS ONE
10
e0125229
2015
-
-
1
-
1
-
-
4
-
4
2
2
-
5
-
-
1
-
-
-
-
-
4
1
1
1
2
4
1
-
-
1
-
-
-
-
-
1
1
-
1
-
-
-
-
4
-
4
2
2
-
-
-
1
-
-
-
-
4
1
1
1
2
4
1
-
-
-
-
1
1
-
4
4
741414
Wang
Novel type II and monomeric NA ...
Campylobacter curvus, Campylobacter curvus 525.92, Campylobacter sp., Campylobacter sp. FOBRC14, Micromonas commoda, Micromonas commoda RCC299, Ostreococcus sp. 'lucimarinus', Ostreococcus sp. 'lucimarinus' CCE9901
Sci. Rep.
5
9150
2015
-
-
4
-
3
-
5
12
-
11
4
10
-
15
-
-
2
-
-
-
4
-
18
4
5
-
2
12
6
-
-
4
-
-
-
-
-
4
5
-
3
-
-
5
-
12
-
11
4
10
-
-
-
2
-
-
4
-
18
5
5
-
2
12
6
-
-
-
-
8
9
-
12
12
741407
Yamada
NAD-dependent isocitrate dehyd ...
Homo sapiens
Sci. Rep.
4
5952
2014
-
-
1
-
1
-
1
-
1
-
-
1
-
2
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
741458
Yang
The role of NAD+-dependent iso ...
Homo sapiens, Mus musculus, Rattus norvegicus
Toxicol. Lett.
224
371-379
2014
-
-
3
-
3
-
-
-
3
-
-
3
-
4
-
-
-
-
-
32
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
3
3
-
3
-
-
-
-
-
3
-
-
3
-
-
-
-
-
32
-
-
3
-
-
-
-
-
-
-
-
-
3
6
6
3
-
-
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
-
-
-
-
2
1
1
1
2
10
1
1
-
-
-
2
2
-
10
10
721381
Yang
Characterization of the mitoch ...
Rhodotorula toruloides, Rhodotorula toruloides AS 2.1389
Appl. Microbiol. Biotechnol.
94
1095-1105
2012
-
-
1
-
-
-
-
-
3
-
-
4
-
9
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
2
-
-
-
-
-
-
-
4
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
721433
McAlister-Henn
Ligand binding and structural ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
519
112-117
2012
1
-
-
-
7
-
-
-
-
1
-
1
-
2
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
7
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
1
1
-
-
-
722295
Wang
Biochemical and molecular char ...
Zymomonas mobilis, Zymomonas mobilis ATCC 10988
FEMS Microbiol. Lett.
327
134-141
2012
-
-
1
-
-
-
5
4
-
4
2
2
-
5
-
-
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
721650
Lin
Basis for half-site ligand bin ...
Saccharomyces cerevisiae
Biochemistry
50
8241-8250
2011
2
-
1
-
4
-
1
18
-
1
2
1
-
2
-
-
1
-
-
-
-
-
1
2
1
-
-
-
1
-
-
1
-
-
-
2
-
1
1
-
4
-
-
1
-
18
-
1
2
1
-
-
-
1
-
-
-
-
1
2
1
-
-
-
1
-
-
-
-
1
1
-
-
-
712440
Dange
Each conserved active site tyr ...
Homo sapiens
J. Biol. Chem.
285
20520-20525
2010
1
-
1
-
7
-
-
12
2
1
-
1
-
2
-
-
1
-
-
-
-
-
2
1
1
-
-
-
1
-
-
1
-
-
-
1
-
1
1
-
7
-
-
-
-
12
2
1
-
1
-
-
-
1
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
713076
Sienkiewicz-Porzucek
Mild reductions in mitochondri ...
Solanum lycopersicum
Mol. Plant
3
156-173
2010
-
-
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
PLoS ONE
5
e9991
2010
-
-
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
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
2
-
-
1
-
-
-
-
2
-
-
-
-
1
-
-
-
-
2
1
-
-
-
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712180
Kang
Mutational analysis of IDH1 co ...
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Int. J. Cancer
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Suppression of metabolic defec ...
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Taylor
Allosteric motions in structur ...
Saccharomyces cerevisiae
J. Biol. Chem.
283
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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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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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2
1
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700359
Hartong
Novel insights into the contri ...
Homo sapiens
Nat. Genet.
40
1230-1234
2008
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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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5
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1
1
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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
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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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689578
Lemaitre
NAD-dependent isocitrate dehyd ...
Arabidopsis thaliana
Plant Physiol.
144
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2007
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667098
Hu
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Crystallization and preliminar ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
F62
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Hu
Novel allosteric properties pr ...
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Arch. Biochem. Biophys.
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2006
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1
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12
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Physiological consequences of ...
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1
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6
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3
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2
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1
1
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669477
Soundar
Identification of Mn2+-binding ...
Homo sapiens
J. Biol. Chem.
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7
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Lemaitre
Expression analysis of Arabido ...
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1
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1
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1
1
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5
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11
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87
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1
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670847
Kalinina
Amino acid residues that deter ...
Escherichia coli
Proteins
64
1001-1009
2006
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1
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-
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660907
Miyazaki
Bifunctional isocitrate-homois ...
Pyrococcus horikoshii
Biochem. Biophys. Res. Commun.
331
341-346
2005
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1
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3
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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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3
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1
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1
1
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3
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2
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1
1
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1
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2
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3
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667647
Anderson
Analysis of interactions with ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae MMY011
Biochemistry
44
16776-16784
2005
1
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1
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1
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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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2
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670158
Watanabe
Elucidation of stability deter ...
Azotobacter vinelandii, Colwellia maris
Microbiology
151
1083-1094
2005
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2
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2
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2
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2
2
2
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4
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2
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2
2
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4
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4
2
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2
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2
-
2
2
2
-
-
4
-
-
-
-
-
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-
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670544
Abiko
Localization of NAD-isocitrate ...
Oryza sativa
Plant Cell Physiol.
46
1724-1734
2005
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-
-
-
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1
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1
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1
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1
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1
-
-
-
-
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-
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-
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670805
Rodriguez-Arnedo
Complete reversal of coenzyme ...
Escherichia coli
Protein J.
24
259-266
2005
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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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1
3
2
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2
2
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1
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4
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2
1
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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1
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3
1
2
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1
2
2
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1
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4
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2
1
1
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-
1
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657111
Lin
-
Characterization of a mutation ...
Arabidopsis thaliana, Arabidopsis thaliana Landsberg
Plant Sci.
166
983-988
2004
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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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6
2
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4
1
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1
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1
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1
1
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1
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1
1
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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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1
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-
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654843
Igamberdiev
Regulation of NAD- and NADP-de ...
Pisum sativum
Biochim. Biophys. Acta
1606
117-125
2003
1
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3
2
1
1
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1
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1
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1
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1
2
1
2
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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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3
2
2
1
1
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1
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1
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1
2
1
2
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1
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654914
Pinheiro de Carvalho
-
Effect of metabolites of gamma ...
Pisum sativum, Zea mays
Biol. Bull.
30
236-242
2003
1
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7
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1
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2
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2
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2
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2
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7
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1
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2
2
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2
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2
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656118
Lin
Homologous binding sites in ye ...
Saccharomyces cerevisiae
J. Biol. Chem.
278
12864-12872
2003
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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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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
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2003
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1
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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3
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11
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1
1
1
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1
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3
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1
1
1
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1
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654652
Anderson
Effect of AMP on mRNA binding ...
Saccharomyces cerevisiae
Biochemistry
41
7065-7073
2002
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2
1
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1
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3
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1
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655607
Inoue
Biochemical and molecular char ...
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127-132
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1
2
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3
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1
2
2
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1
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1
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2
1
1
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1
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656052
Lin
Isocitrate binding at two func ...
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J. Biol. Chem.
277
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1
2
2
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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6
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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
2
1
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1
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721450
Steen
Identification of cofactor dis ...
Pyrococcus furiosus
Arch. Microbiol.
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297-300
2002
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6
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1
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3
6
1
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2
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6
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2
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1
1
3
6
1
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Subunit interactions of yeast ...
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1
1
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727835
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Comparison of isocitrate dehyd ...
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1
1
1
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2
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286772
Anderson
Allosteric inhibition of NAD+- ...
Saccharomyces cerevisiae
Biochemistry
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2000
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1
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286769
Kim
Identification and functional ...
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2
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1
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286773
Martinez-Rivas
Purification and characterizat ...
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8
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8
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1
1
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1
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286774
McIntosh
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Partial purification and chara ...
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1
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1
1
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1
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286775
Huang
Identification of the subunits ...
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Arch. Biochem. Biophys.
348
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1997
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1
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286776
Alvarez-Villafane
Two NAD+-dependent isocitrate ...
Phycomyces blakesleeanus
Biochemistry
35
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1996
1
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1
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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1
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1
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1
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2
2
1
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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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-
286777
Hurley
Determinants of cofactor speci ...
Escherichia coli
Biochemistry
35
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1996
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1
1
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4
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1
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2
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1
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4
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1
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1
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663920
Mitchell
-
Identification of a multienzym ...
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1996
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1
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1
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-
286770
Gabriel
Kinetic regulation of yeast NA ...
Saccharomyces cerevisiae
Biochemistry
30
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1991
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16
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1
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1
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16
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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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286767
Rutter
Regulation of NAD+-linked isoc ...
Rattus norvegicus
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1988
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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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2
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1
-
1
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-
-
-
-
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286764
Gabriel
Inhibition and activation of b ...
Bos taurus
Arch. Biochem. Biophys.
240
128-134
1985
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3
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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
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1
-
-
-
-
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-
-
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-
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286765
Gabriel
NAD-specific isocitrate dehydr ...
Bos taurus
Biochem. J.
229
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1985
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6
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1
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1
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1
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6
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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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-
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-
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286766
Evans
-
The role of the mitochondrial ...
Rhodotorula toruloides
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31
845-850
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6
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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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6
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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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-
1
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1
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-
-
-
-
-
-
-
-
286762
Gabriel
Inhibition of bovine heart NAD ...
Bos taurus
Biochemistry
23
2773-2778
1984
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-
-
-
-
-
2
-
1
1
-
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
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2
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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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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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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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1
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1
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-
1
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-
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286768
Gabriel
Citrate activation of NAD-spec ...
Bos taurus
J. Biol. Chem.
259
1622-1628
1984
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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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286761
Tezuka
Isolation and characterization ...
Solanum tuberosum
Plant Physiol.
72
959-963
1982
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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
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2
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2
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1
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1
-
1
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286758
Willson
The activation of ox-brain NAD ...
Bos taurus
Eur. J. Biochem.
113
477-483
1981
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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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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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286759
Ehrlich
Re-evaluation of molecular wei ...
Sus scrofa
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256
10560-10564
1981
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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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2
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1
1
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286760
Gabriel
Specific site inhibitors of NA ...
Bos taurus
J. Biol. Chem.
257
8021-8029
1981
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5
1
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2
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1
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1
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5
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1
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1
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2
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1
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286756
Hoffmann
Regulation of NAD+- and NADP+- ...
Pseudomonas sp., Pseudomonas sp. W 6
Z. Allg. Mikrobiol.
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399-404
1980
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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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1
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2
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1
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2
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1
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286757
Willson
The effect of pH on the allost ...
Bos taurus
Eur. J. Biochem.
109
411-416
1980
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1
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1
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1
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1
1
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
-
1
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1
1
1
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286755
Ramachandran
Evidence for the presence of t ...
Sus scrofa
Proc. Natl. Acad. Sci. USA
75
252-255
1978
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3
1
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1
1
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2
1
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1
1
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1
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1
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3
1
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1
1
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2
1
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1
1
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286754
Nabeshima
-
Partial purification and some ...
Candida tropicalis
Agric. Biol. Chem.
41
509-516
1977
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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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1
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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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-
-
1
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-
-
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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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7
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7
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7
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7
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8
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7
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7
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7
-
7
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7
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7
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-
7
-
7
-
-
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8
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286751
Cohen
Role of manganous ion in the k ...
Sus scrofa
Eur. J. Biochem.
47
35-45
1974
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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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4
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1
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1
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1
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1
1
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1
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286752
Silinski
The kinetics of NAD-linked iso ...
Bos taurus
Biochim. Biophys. Acta
370
1-25
1974
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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
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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
1
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1
1
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1
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286750
Glaeser
NADP- und NAD-spezifische dehy ...
Cupriavidus necator
Arch. Microbiol.
86
327-337
1972
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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
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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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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. , Myrbäck, K. , eds. )
7
105-126
1963
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3
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