BRENDA - Enzyme Database show
show all sequences of 1.1.1.39

Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction

Aktas, D.F.; Cook, P.F.; Biochemistry 47, 2539-2546 (2008)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
N434A
site-directed mutagenesis, the interaction of the 434 position residue with malate is lost in the mutant, causing malate to reorient itself, leading to a slower decarboxylation
Ascaris suum
N434E
site-directed mutagenesis, the longer glutamine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
Ascaris suum
N434M
site-directed mutagenesis, the longer methionine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
Ascaris suum
N479Q
site-directed mutagenesis, the stepwise oxidative decarboxylation mechanism observed for the wild-type enzyme changed to a concerted one, which is totally rate limiting, for the N479Q mutant enzyme
Ascaris suum
N479S
site-directed mutagenesis, the mutant with the shorter serine side chain shows very similar values of KNAD+, Kmalate, and isotope effects relative to the wild-type enzyme, but V/Et is decreased 2000fold due to an increased freedom of rotation, resulting in nonproductively bound cofactor
Ascaris suum
S433A
site-directed mutagenesis, KNAD+ for the S433A mutant enzyme is increased by 80fold compared to the wild-type enzyme
Ascaris suum
S433C
site-directed mutagenesis, the mutant enzyme exhibits 9fold and 500fold increases in Kmalate and KNAD, respectively, compared to the wild-type enzyme
Ascaris suum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
primary deuterium and 13C kinetic isotope effects, kinetics, and kinetic mechanism of wild-type and mutant enzymes, overview
Ascaris suum
0.5
-
(S)-malate
pH 7.0, 25C, mutant N434A, in presence of Mn2+
Ascaris suum
0.8
-
NAD+
pH 7.0, 25C, wild-type enzyme
Ascaris suum
0.8
-
(S)-malate
pH 7.0, 25C, wild-type enzyme
Ascaris suum
1.3
-
(S)-malate
pH 7.0, 25C, mutant S433A
Ascaris suum
1.6
-
NAD+
pH 7.0, 25C, mutant S433A
Ascaris suum
1.7
-
NAD+
pH 7.0, 25C, mutant N479S
Ascaris suum
1.7
-
(S)-malate
pH 7.0, 25C, mutant N479S
Ascaris suum
1.8
-
NAD+
pH 7.0, 25C, mutant N479Q
Ascaris suum
1.8
-
(S)-malate
pH 7.0, 25C, mutant N479Q
Ascaris suum
2
-
NAD+
pH 7.0, 25C, mutant N434A, in presence of Mn2+
Ascaris suum
2.2
-
(S)-malate
pH 7.0, 25C, mutant N434M
Ascaris suum
3
-
NAD+
pH 7.0, 25C, mutant N434M
Ascaris suum
4.3
-
(S)-malate
pH 7.0, 25C, mutant N434Q
Ascaris suum
5
-
NAD+
pH 7.0, 25C, mutant N434Q
Ascaris suum
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Ascaris suum
5739
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
activates mutant N434A
Ascaris suum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Ascaris suum
-
pyruvate + CO2 + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ascaris suum
-
-
-
Reaction
Reaction
Commentary
Organism
(S)-malate + NAD+ = pyruvate + CO2 + NADH
acid-base chemical mechanism for Ascaris suum malic enzyme
Ascaris suum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
-
685215
Ascaris suum
pyruvate + CO2 + NADH
-
-
-
r
(S)-malate + NAD+
the mitochondrial NAD-malic enzyme catalyzes the oxidative decarboxylation of malate to pyruvate and CO2
685215
Ascaris suum
pyruvate + CO2 + NADH
-
-
-
r
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Ascaris suum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Ascaris suum
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
binding structure, overview
Ascaris suum
NADH
-
Ascaris suum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
binding structure, overview
Ascaris suum
NADH
-
Ascaris suum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
N434A
site-directed mutagenesis, the interaction of the 434 position residue with malate is lost in the mutant, causing malate to reorient itself, leading to a slower decarboxylation
Ascaris suum
N434E
site-directed mutagenesis, the longer glutamine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
Ascaris suum
N434M
site-directed mutagenesis, the longer methionine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme
Ascaris suum
N479Q
site-directed mutagenesis, the stepwise oxidative decarboxylation mechanism observed for the wild-type enzyme changed to a concerted one, which is totally rate limiting, for the N479Q mutant enzyme
Ascaris suum
N479S
site-directed mutagenesis, the mutant with the shorter serine side chain shows very similar values of KNAD+, Kmalate, and isotope effects relative to the wild-type enzyme, but V/Et is decreased 2000fold due to an increased freedom of rotation, resulting in nonproductively bound cofactor
Ascaris suum
S433A
site-directed mutagenesis, KNAD+ for the S433A mutant enzyme is increased by 80fold compared to the wild-type enzyme
Ascaris suum
S433C
site-directed mutagenesis, the mutant enzyme exhibits 9fold and 500fold increases in Kmalate and KNAD, respectively, compared to the wild-type enzyme
Ascaris suum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
primary deuterium and 13C kinetic isotope effects, kinetics, and kinetic mechanism of wild-type and mutant enzymes, overview
Ascaris suum
0.5
-
(S)-malate
pH 7.0, 25C, mutant N434A, in presence of Mn2+
Ascaris suum
0.8
-
NAD+
pH 7.0, 25C, wild-type enzyme
Ascaris suum
0.8
-
(S)-malate
pH 7.0, 25C, wild-type enzyme
Ascaris suum
1.3
-
(S)-malate
pH 7.0, 25C, mutant S433A
Ascaris suum
1.6
-
NAD+
pH 7.0, 25C, mutant S433A
Ascaris suum
1.7
-
NAD+
pH 7.0, 25C, mutant N479S
Ascaris suum
1.7
-
(S)-malate
pH 7.0, 25C, mutant N479S
Ascaris suum
1.8
-
NAD+
pH 7.0, 25C, mutant N479Q
Ascaris suum
1.8
-
(S)-malate
pH 7.0, 25C, mutant N479Q
Ascaris suum
2
-
NAD+
pH 7.0, 25C, mutant N434A, in presence of Mn2+
Ascaris suum
2.2
-
(S)-malate
pH 7.0, 25C, mutant N434M
Ascaris suum
3
-
NAD+
pH 7.0, 25C, mutant N434M
Ascaris suum
4.3
-
(S)-malate
pH 7.0, 25C, mutant N434Q
Ascaris suum
5
-
NAD+
pH 7.0, 25C, mutant N434Q
Ascaris suum
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Ascaris suum
5739
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
activates mutant N434A
Ascaris suum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Ascaris suum
-
pyruvate + CO2 + NADH
-
-
r
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
-
685215
Ascaris suum
pyruvate + CO2 + NADH
-
-
-
r
(S)-malate + NAD+
the mitochondrial NAD-malic enzyme catalyzes the oxidative decarboxylation of malate to pyruvate and CO2
685215
Ascaris suum
pyruvate + CO2 + NADH
-
-
-
r
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Ascaris suum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Ascaris suum
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
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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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722082
Niedzwiecka
Purification and properties of ...
Clupea harengus
Comp. Biochem. Physiol. B
164
216-220
2013
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5
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1
1
1
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6
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1
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5
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1
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1
2
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2
1
1
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2
2
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721353
Zhang
NAD(P)+-malic enzyme mutants o ...
Azorhizobium caulinodans, Sinorhizobium sp., Sinorhizobium sp. NGR234
Appl. Environ. Microbiol.
78
2803-2812
2012
4
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1
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1
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2
6
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5
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13
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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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3
3
-
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-
721357
Rodriguez
Impact of malic enzymes on ant ...
Streptomyces coelicolor, Streptomyces coelicolor M145
Appl. Environ. Microbiol.
78
4571-4579
2012
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1
-
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2
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1
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2
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4
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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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2
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2
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1
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1
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2
2
-
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721778
Fu
-
The effects of abiotic stresse ...
Triticum aestivum, Triticum aestivum Jinmai 47
Biol. Plant.
55
196-200
2011
-
-
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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2
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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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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
-
-
723540
Hsieh
Determinants of nucleotide-bin ...
Ascaris suum
PLoS ONE
6
e25312
2011
-
-
-
-
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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710948
Landete
Requirement of the Lactobacill ...
Lactobacillus casei, Lactobacillus casei BL23 and ATCC 334
Appl. Environ. Microbiol.
76
84-95
2010
-
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1
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2
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2
3
3
2
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711147
Tronconi
NAD-malic enzymes of Arabidops ...
Arabidopsis thaliana
Biochem. J.
430
295-303
2010
-
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1
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1
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7
3
1
1
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2
-
4
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1
1
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3
1
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2
1
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1
10
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2
2
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2
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11
10
4
2
2
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2
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2
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3
2
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2
2
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2
4
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711524
Sato
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Rhodopseudomonas palustris, Rhodopseudomonas palustris No. 7
Biosci. Biotechnol. Biochem.
74
75-81
2010
-
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1
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7
5
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6
2
4
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2
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1
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1
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2
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3
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7
2
5
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6
2
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1
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1
1
6
1
1
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2
4
1
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1
1
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2
2
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4
4
712417
Tronconi
Three different and tissue-spe ...
Arabidopsis thaliana
J. Biol. Chem.
285
11870-11879
2010
8
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1
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1
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5
2
1
1
3
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5
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1
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4
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9
1
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6
3
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1
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21
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3
3
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2
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9
3
3
1
3
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3
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12
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9
3
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6
3
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1
3
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6
6
713373
Ren
Induction of erythroid differe ...
Homo sapiens
PLoS ONE
5
e12520
2010
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1
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712942
Pongratz
Investigating the roles of mit ...
Rattus norvegicus
Methods Enzymol.
457
425-450
2009
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1
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2
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713212
Rzepka
-
Effect of abiotic stress facto ...
Mnium undulatum, Pilosella officinarum, Polytrichum commune, Polytrichum piliferum
Photosynthetica
47
141-145
2009
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4
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8
4
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8
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4
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4
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4
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8
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4
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4
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685215
Aktas
Proper positioning of the nico ...
Ascaris suum
Biochemistry
47
2539-2546
2008
-
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7
-
-
15
1
1
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1
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1
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1
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2
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1
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1
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2
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2
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7
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15
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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685678
Ohno
Reverse reaction of malic enzy ...
Brevundimonas diminuta, Brevundimonas diminuta IFO 13182
Biosci. Biotechnol. Biochem.
72
1278-1282
2008
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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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689604
Tronconi
Arabidopsis NAD-malic enzyme f ...
Arabidopsis thaliana
Plant Physiol.
146
1540-1552
2008
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1
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2
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654720
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Ascaris suum NAD-malic enzyme ...
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657362
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Homo sapiens
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Alternative substrates for mal ...
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Crystal structure of the malic ...
Ascaris suum
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286706
Voegele
Characterization of two member ...
Sinorhizobium meliloti
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286720
Chen
Purification and characterizat ...
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286719
Farias de Aragao
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Purification and partial chara ...
Vigna unguiculata
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1
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286717
Hrdy
Purification and partial chara ...
Tritrichomonas suis
Parasitology
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286718
Suye
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Purification and properties of ...
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2
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286701
Willeford
pH Effects on the activity and ...
Solanum tuberosum
Plant Physiol.
84
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1987
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286702
Willeford
Evidence for a multiple subuni ...
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286703
Willeford
Regulation of the NAD malic en ...
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286700
Artus
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NAD-malic enzyme from plants ...
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Day
Activation of NAD-linked malic ...
Brassica oleracea, Solanum tuberosum
Arch. Biochem. Biophys.
231
233-242
1984
2
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4
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286705
Canellas
Kinetic properties of NAD mali ...
Brassica oleracea
Arch. Biochem. Biophys.
229
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1984
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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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286707
Wedding
Physical and kinetic propertie ...
Crassula argentea
Plant Physiol.
72
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1983
6
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7
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2
4
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6
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2
4
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-
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286708
Hatch
Determination of NAD malic enz ...
Amaranthus retroflexus
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1
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286709
Wedding
Slow transients in the activit ...
Crassula argentea
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1981
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2
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1
-
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1
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-
-
-
2
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286710
Grover
Purification of NAD malic enzy ...
Solanum tuberosum
Arch. Biochem. Biophys.
209
396-407
1981
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8
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3
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1
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2
1
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3
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2
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-
-
-
2
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-
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8
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2
3
-
-
-
-
1
-
1
1
-
2
1
-
-
-
1
3
-
-
-
-
-
-
-
-
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286711
Canellas
Substrate and metal ion intera ...
Brassica oleracea
Arch. Biochem. Biophys.
199
259-264
1980
-
-
-
-
-
-
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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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-
-
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-
1
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-
-
-
-
2
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-
-
-
-
-
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-
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-
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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
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12
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1
1
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12
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-
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12
-
-
-
-
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2
2
2
-
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-
-
-
-
-
1
1
-
12
-
-
-
-
-
1
1
-
-
-
-
-
-
-
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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
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1
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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
-
-
4
-
-
1
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4
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1
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6
1
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-
-
-
1
-
3
-
1
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
286714
Mounib
NAD- and NADP-malic enzymes in ...
Bos taurus, Gadidae, Homo sapiens, salmon
FEBS Lett.
48
79-84
1974
-
-
-
-
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-
-
-
-
-
-
4
-
-
-
-
-
4
-
-
4
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
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
-
-
1
-
-
1
-
-
1
-
-
3
-
-
-
-
-
1
-
-
2
-
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-
-
-
-
2
-
-
-
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2
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8
1
2
1
-
-
-
-
1
-
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
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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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