BRENDA - Enzyme Database show
show all sequences of 1.1.1.39

Isolation and properties of malic enzyme and its gene in Rhodopseudomonas palustris No. 7

Sato, I.; Yoshikawa, J.; Furusawa, A.; Chiku, K.; Amachi, S.; Fujii, T.; Biosci. Biotechnol. Biochem. 74, 75-81 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
Rhodopseudomonas palustris
Inhibitors
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
enzyme activity is allosterically regulated by acetyl-CoA, almost complete inhibition at 0.05 mM
Rhodopseudomonas palustris
Ca2+
inhibits 30% at 1 mM and 60% at 10 mM
Rhodopseudomonas palustris
EDTA
complete inhibition at 0.1 mM
Rhodopseudomonas palustris
fructose 6-phosphate
competitive versus (S)-malate, 70% inhibition at 2.5 mM
Rhodopseudomonas palustris
Li+
slight inhibition
Rhodopseudomonas palustris
Na+
complete inhibition at 10 mM, no effect by Na+ at 1 mM
Rhodopseudomonas palustris
oxaloacetate
competitive versus (S)-malate, 20% inhibition at 2.5 mM
Rhodopseudomonas palustris
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics, overview
Rhodopseudomonas palustris
0.11
-
NAD+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
1.7
-
(S)-malate
pH 7.2, 30C, with NAD+
Rhodopseudomonas palustris
1.8
-
NADP+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
15
-
(S)-malate
pH 7.2, 30C, with NADP+
Rhodopseudomonas palustris
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
activates 7fold at 1-10 mM
Rhodopseudomonas palustris
Mg2+
activates 12fold at 1 mM and 15fold at 10 mM
Rhodopseudomonas palustris
Mn2+
activates 13fold at 1 mM and 15fold at 10 mM
Rhodopseudomonas palustris
additional information
malic enzyme activity is markedly enhanced by mono- and divalent cations
Rhodopseudomonas palustris
NH4+
activates 12fold at 1 mM and 20fold at 10 mM
Rhodopseudomonas palustris
Zn2+
5fold activation at 5 mM, only slight activation at 10 mM
Rhodopseudomonas palustris
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
86000
-
x * 86000
Rhodopseudomonas palustris
650000
-
-
Rhodopseudomonas palustris
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Rhodopseudomonas palustris
-
pyruvate + NADH + H+ + CO2
-
-
?
(S)-malate + NAD+
Rhodopseudomonas palustris No. 7
-
pyruvate + NADH + H+ + CO2
-
-
?
(S)-malate + NADP+
Rhodopseudomonas palustris
NADP+ shows 22% of the activity with NAD+
pyruvate + NADPH + H+ + CO2
-
-
?
(S)-malate + NADP+
Rhodopseudomonas palustris No. 7
NADP+ shows 22% of the activity with NAD+
pyruvate + NADPH + H+ + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodopseudomonas palustris
A4F2S6
-
-
Rhodopseudomonas palustris No. 7
A4F2S6
-
-
Purification (Commentary)
Commentary
Organism
native enzyme 1500fold to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, adsorption chromatography, ultrafiltration, and gel filtration
Rhodopseudomonas palustris
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
64
-
purified enzyme, pH 7.2, 30C
Rhodopseudomonas palustris
Storage Stability
Storage Stability
Organism
-80C, purified native enzyme, 8 months, completely stable
Rhodopseudomonas palustris
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
-
711524
Rhodopseudomonas palustris
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NAD+
-
711524
Rhodopseudomonas palustris No. 7
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NADP+
NADP+ shows 22% of the activity with NAD+
711524
Rhodopseudomonas palustris
pyruvate + NADPH + H+ + CO2
-
-
-
?
(S)-malate + NADP+
NADP+ shows 22% of the activity with NAD+
711524
Rhodopseudomonas palustris No. 7
pyruvate + NADPH + H+ + CO2
-
-
-
?
additional information
the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate
711524
Rhodopseudomonas palustris
?
-
-
-
-
additional information
the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate
711524
Rhodopseudomonas palustris No. 7
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
oligomer
x * 86000
Rhodopseudomonas palustris
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
-
Rhodopseudomonas palustris
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
purified enzyme, stable up to, loss of activity above
Rhodopseudomonas palustris
70
-
purified enzyme, almost complete inactivation
Rhodopseudomonas palustris
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
480
-
(S)-malate
pH 7.2, 30C, with NADP+
Rhodopseudomonas palustris
520
-
NADP+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
720
-
NAD+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
770
-
(S)-malate
pH 7.2, 30C, with NAD+
Rhodopseudomonas palustris
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Rhodopseudomonas palustris
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
8
-
purified enzyme, most stable at
Rhodopseudomonas palustris
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the enzyme uses both NAD+ and NADP+
Rhodopseudomonas palustris
NAD+
preferred cofactor
Rhodopseudomonas palustris
NADP+
-
Rhodopseudomonas palustris
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.36
-
oxaloacetate
pH 7.2, 30C, versus (S)-malate
Rhodopseudomonas palustris
7.4
-
fructose 6-phosphate
pH 7.2, 30C, versus (S)-malate
Rhodopseudomonas palustris
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Rhodopseudomonas palustris
sequence calculation
-
6.3
Cloned(Commentary) (protein specific)
Commentary
Organism
DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
Rhodopseudomonas palustris
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the enzyme uses both NAD+ and NADP+
Rhodopseudomonas palustris
NAD+
preferred cofactor
Rhodopseudomonas palustris
NADP+
-
Rhodopseudomonas palustris
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
acetyl-CoA
enzyme activity is allosterically regulated by acetyl-CoA, almost complete inhibition at 0.05 mM
Rhodopseudomonas palustris
Ca2+
inhibits 30% at 1 mM and 60% at 10 mM
Rhodopseudomonas palustris
EDTA
complete inhibition at 0.1 mM
Rhodopseudomonas palustris
fructose 6-phosphate
competitive versus (S)-malate, 70% inhibition at 2.5 mM
Rhodopseudomonas palustris
Li+
slight inhibition
Rhodopseudomonas palustris
Na+
complete inhibition at 10 mM, no effect by Na+ at 1 mM
Rhodopseudomonas palustris
oxaloacetate
competitive versus (S)-malate, 20% inhibition at 2.5 mM
Rhodopseudomonas palustris
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.36
-
oxaloacetate
pH 7.2, 30C, versus (S)-malate
Rhodopseudomonas palustris
7.4
-
fructose 6-phosphate
pH 7.2, 30C, versus (S)-malate
Rhodopseudomonas palustris
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics, overview
Rhodopseudomonas palustris
0.11
-
NAD+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
1.7
-
(S)-malate
pH 7.2, 30C, with NAD+
Rhodopseudomonas palustris
1.8
-
NADP+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
15
-
(S)-malate
pH 7.2, 30C, with NADP+
Rhodopseudomonas palustris
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
activates 7fold at 1-10 mM
Rhodopseudomonas palustris
Mg2+
activates 12fold at 1 mM and 15fold at 10 mM
Rhodopseudomonas palustris
Mn2+
activates 13fold at 1 mM and 15fold at 10 mM
Rhodopseudomonas palustris
additional information
malic enzyme activity is markedly enhanced by mono- and divalent cations
Rhodopseudomonas palustris
NH4+
activates 12fold at 1 mM and 20fold at 10 mM
Rhodopseudomonas palustris
Zn2+
5fold activation at 5 mM, only slight activation at 10 mM
Rhodopseudomonas palustris
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
86000
-
x * 86000
Rhodopseudomonas palustris
650000
-
-
Rhodopseudomonas palustris
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Rhodopseudomonas palustris
-
pyruvate + NADH + H+ + CO2
-
-
?
(S)-malate + NAD+
Rhodopseudomonas palustris No. 7
-
pyruvate + NADH + H+ + CO2
-
-
?
(S)-malate + NADP+
Rhodopseudomonas palustris
NADP+ shows 22% of the activity with NAD+
pyruvate + NADPH + H+ + CO2
-
-
?
(S)-malate + NADP+
Rhodopseudomonas palustris No. 7
NADP+ shows 22% of the activity with NAD+
pyruvate + NADPH + H+ + CO2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme 1500fold to homogeneity by ammonium sulfate fractionation, anion exchange and hydrophobic interaction chromatography, adsorption chromatography, ultrafiltration, and gel filtration
Rhodopseudomonas palustris
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
64
-
purified enzyme, pH 7.2, 30C
Rhodopseudomonas palustris
Storage Stability (protein specific)
Storage Stability
Organism
-80C, purified native enzyme, 8 months, completely stable
Rhodopseudomonas palustris
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
-
711524
Rhodopseudomonas palustris
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NAD+
-
711524
Rhodopseudomonas palustris No. 7
pyruvate + NADH + H+ + CO2
-
-
-
?
(S)-malate + NADP+
NADP+ shows 22% of the activity with NAD+
711524
Rhodopseudomonas palustris
pyruvate + NADPH + H+ + CO2
-
-
-
?
(S)-malate + NADP+
NADP+ shows 22% of the activity with NAD+
711524
Rhodopseudomonas palustris No. 7
pyruvate + NADPH + H+ + CO2
-
-
-
?
additional information
the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate
711524
Rhodopseudomonas palustris
?
-
-
-
-
additional information
the enzyme shows 1% of the forward reaction activity in the reverse reaction and in decarboxylation oxaloacetate. D-malate and succinate are poor substrates showing 3.9% and 8.2% of the activity with (S)-malate
711524
Rhodopseudomonas palustris No. 7
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
oligomer
x * 86000
Rhodopseudomonas palustris
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
-
Rhodopseudomonas palustris
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
purified enzyme, stable up to, loss of activity above
Rhodopseudomonas palustris
70
-
purified enzyme, almost complete inactivation
Rhodopseudomonas palustris
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
480
-
(S)-malate
pH 7.2, 30C, with NADP+
Rhodopseudomonas palustris
520
-
NADP+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
720
-
NAD+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
770
-
(S)-malate
pH 7.2, 30C, with NAD+
Rhodopseudomonas palustris
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Rhodopseudomonas palustris
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
8
-
purified enzyme, most stable at
Rhodopseudomonas palustris
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Rhodopseudomonas palustris
sequence calculation
-
6.3
General Information
General Information
Commentary
Organism
additional information
enzyme activity is allosterically regulated by acetyl-CoA
Rhodopseudomonas palustris
physiological function
malic enzyme plays an important role in the metabolic regulation under photoheterotrophic conditions, carbon metabolic pathway, overview
Rhodopseudomonas palustris
General Information (protein specific)
General Information
Commentary
Organism
additional information
enzyme activity is allosterically regulated by acetyl-CoA
Rhodopseudomonas palustris
physiological function
malic enzyme plays an important role in the metabolic regulation under photoheterotrophic conditions, carbon metabolic pathway, overview
Rhodopseudomonas palustris
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2900
-
NADP+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
3100
-
(S)-malate
pH 7.2, 30C, with NAD+
Rhodopseudomonas palustris
3300
-
(S)-malate
pH 7.2, 30C, with NADP+
Rhodopseudomonas palustris
6900
-
NAD+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
2900
-
NADP+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
3100
-
(S)-malate
pH 7.2, 30C, with NAD+
Rhodopseudomonas palustris
3300
-
(S)-malate
pH 7.2, 30C, with NADP+
Rhodopseudomonas palustris
6900
-
NAD+
pH 7.2, 30C, with (S)-malate
Rhodopseudomonas palustris
Other publictions for EC 1.1.1.39
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)
738272
Niedzwiecka
NAD-preferring malic enzyme: l ...
Clupea harengus
Fish Physiol. Biochem.
43
351-360
2017
-
-
-
-
-
-
1
-
1
-
-
1
-
2
-
-
-
-
-
1
-
-
1
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
722082
Niedzwiecka
Purification and properties of ...
Clupea harengus
Comp. Biochem. Physiol. B
164
216-220
2013
-
-
-
-
-
-
-
5
-
1
1
1
-
6
-
-
1
-
-
1
2
-
2
1
1
-
-
-
2
2
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
5
-
1
1
1
-
-
-
1
-
1
2
-
2
1
1
-
-
-
2
2
-
-
-
-
-
-
-
-
721353
Zhang
NAD(P)+-malic enzyme mutants o ...
Azorhizobium caulinodans, Sinorhizobium sp., Sinorhizobium sp. NGR234
Appl. Environ. Microbiol.
78
2803-2812
2012
4
-
1
-
1
-
2
6
-
-
-
5
-
13
-
-
1
-
-
-
1
-
5
-
1
-
-
-
1
-
-
4
-
-
-
4
-
1
4
-
1
-
-
2
-
6
-
-
-
5
-
-
-
1
-
-
1
-
5
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
721357
Rodriguez
Impact of malic enzymes on ant ...
Streptomyces coelicolor, Streptomyces coelicolor M145
Appl. Environ. Microbiol.
78
4571-4579
2012
-
-
1
-
-
-
-
2
-
1
-
2
-
4
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
1
-
2
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
721778
Fu
-
The effects of abiotic stresse ...
Triticum aestivum, Triticum aestivum Jinmai 47
Biol. Plant.
55
196-200
2011
-
-
1
-
-
-
-
-
1
-
-
2
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
723540
Hsieh
Determinants of nucleotide-bin ...
Ascaris suum
PLoS ONE
6
e25312
2011
-
-
-
-
1
-
-
-
1
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710948
Landete
Requirement of the Lactobacill ...
Lactobacillus casei, Lactobacillus casei BL23 and ATCC 334
Appl. Environ. Microbiol.
76
84-95
2010
-
-
1
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
2
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2
-
-
-
-
2
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-
2
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2
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-
-
-
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2
-
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4
-
-
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-
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-
-
-
-
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-
-
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-
286705
Canellas
Kinetic properties of NAD mali ...
Brassica oleracea
Arch. Biochem. Biophys.
229
414-425
1984
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-
-
-
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2
3
-
3
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1
-
-
1
1
-
1
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1
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-
-
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1
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1
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-
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2
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3
-
3
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1
-
1
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-
1
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-
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-
-
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-
-
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-
286707
Wedding
Physical and kinetic propertie ...
Crassula argentea
Plant Physiol.
72
1021-1028
1983
6
-
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-
-
-
5
7
-
2
4
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1
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1
1
-
1
1
-
3
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-
-
-
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2
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6
-
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2
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5
-
7
-
2
4
-
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1
-
1
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
286708
Hatch
Determination of NAD malic enz ...
Amaranthus retroflexus
Plant Physiol.
69
483-491
1982
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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
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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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-
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-
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-
286709
Wedding
Slow transients in the activit ...
Crassula argentea
Plant Physiol.
68
1416-1423
1981
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-
-
-
-
-
-
-
-
2
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1
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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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1
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2
-
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-
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1
-
-
1
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-
-
-
-
2
-
-
-
-
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-
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286710
Grover
Purification of NAD malic enzy ...
Solanum tuberosum
Arch. Biochem. Biophys.
209
396-407
1981
-
-
-
-
-
-
-
8
-
2
3
-
-
1
-
-
1
-
-
1
1
-
2
1
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-
1
3
-
-
2
-
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-
-
-
2
-
-
-
-
-
-
8
-
2
3
-
-
-
-
1
-
1
1
-
2
1
-
-
-
1
3
-
-
-
-
-
-
-
-
-
286711
Canellas
Substrate and metal ion intera ...
Brassica oleracea
Arch. Biochem. Biophys.
199
259-264
1980
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-
-
-
-
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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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2
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286712
Hoek
Nicotinamide-adenine dinucleot ...
Apis mellifera, Glossina austeni, Glossina longipennis, Glossina morsitans, Glossina pallidipes, Heliocarpus sp., Odontotermes sp., Periplaneta americana, Sarcophaga sp., Schistocerca gregaria, Spodoptera exempta
Biochem. J.
160
253-262
1976
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-
-
-
-
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2
2
2
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11
-
-
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-
-
1
1
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12
-
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1
1
-
12
-
-
-
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-
12
-
-
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-
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2
2
2
-
-
-
-
-
-
-
1
1
-
12
-
-
-
-
-
1
1
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-
-
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-
-
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-
286713
Hatch
Properties of leaf NAD malic e ...
Amaranthus edulis, Atriplex spongiosa, Panicum miliaceum
Arch. Biochem. Biophys.
165
188-200
1974
4
-
-
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-
1
4
1
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6
1
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3
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1
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3
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1
4
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2
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4
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4
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4
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1
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4
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1
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6
1
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1
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3
-
1
4
-
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2
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-
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286714
Mounib
NAD- and NADP-malic enzymes in ...
Bos taurus, Gadidae, Homo sapiens, salmon
FEBS Lett.
48
79-84
1974
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-
-
-
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4
-
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4
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4
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4
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4
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4
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4
-
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286715
Lin
Malic enzymes of rabbit heart ...
Oryctolagus cuniculus
J. Biol. Chem.
249
3867-3875
1974
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-
-
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2
8
1
2
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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2
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2
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2
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8
1
2
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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-
286716
Eyzaguirre
Two malic enzymes in Pseudomon ...
Pseudomonas aeruginosa
J. Bacteriol.
116
215-221
1973
-
-
-
-
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1
-
2
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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2
2
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2
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