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show all sequences of 1.1.1.39

NAD-malic enzymes of Arabidopsis thaliana display distinct kinetic mechanisms that support differences in physiological control

Tronconi, M.A.; Gerrard Wheeler, M.C.; Maurino, V.G.; Drincovich, M.F.; Andreo, C.S.; Biochem. J. 430, 295-303 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of NAD-ME1, NAD-ME2, and NAD-MEH; recombinant expression of NAD-ME1, NAD-ME2, and NAD-MEH
Arabidopsis thaliana
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism; construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
Arabidopsis thaliana
Inhibitors
Inhibitors
Commentary
Organism
Structure
(S)-malate
isozyme NAD-ME2, competitive
Arabidopsis thaliana
5'-AMP
isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate
Arabidopsis thaliana
CO2
chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate; isozyme NAD-ME2 and chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate
Arabidopsis thaliana
additional information
product inhibition patterns of isozyme NAD-ME2, overview; product inhibition patterns of isozyme NAD-ME2, overview
Arabidopsis thaliana
NADH
isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate. NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q; NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q
Arabidopsis thaliana
pyruvate
isozyme NAD-ME2, uncompetitive versus NAD+, mixed inhibition versus (S)-malate. Pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q; pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q
Arabidopsis thaliana
Tartrate
substrate analogue, isozyme NAD-ME2, uncompetitive versus NAD+, competitive versus (S)-malate
Arabidopsis thaliana
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Isozyme NAD-ME2 follows a sequential ordered Bi-Ter mechanism. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview; kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
Arabidopsis thaliana
1.1
-
NAD+
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
2.6
-
(S)-malate
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
isozyme NAD-ME1; isozymes NAD-ME1 and NAD-ME2
Arabidopsis thaliana
5739
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mn2+
activates; activates probably
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Arabidopsis thaliana
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
pyruvate + NADH + H+ + CO2
-
-
r
(S)-malate + NAD+
Arabidopsis thaliana
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
pyruvate + NADH + H+ + CO2
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
Q8L7K9
isozyme NAD-ME2
-
Arabidopsis thaliana
Q9T0H6
isozyme NAD-ME1
-
Purification (Commentary)
Commentary
Organism
recombinant NAD-ME1, NAD-ME2, and NAD-MEH; recombinant NAD-ME1, NAD-ME2, and NAD-MEH
Arabidopsis thaliana
Reaction
Reaction
Commentary
Organism
(S)-malate + NAD+ = pyruvate + CO2 + NADH
isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Hetereodimer NAD-MEH can bind both substrates randomly. Interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour; isozyme NAD-ME2 and chimeric mutant NAD-ME1q follow a sequential ordered Bi-Ter mechanism, NAD+ being the leading substrate followed by (S)-malate. Isozyme NAD-ME1 and hetereodimer NAD-MEH can bind both substrates randomly. However, NAD-ME1 shows a preferred route that involves the addition of NAD+ first. interaction between NAD-ME1 and -ME2 generates a heteromeric isozyme NAD-MEH with a particular kinetic behaviour
Arabidopsis thaliana
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
711147
Arabidopsis thaliana
pyruvate + NADH + H+ + CO2
-
-
-
r
(S)-malate + NAD+
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
711147
Arabidopsis thaliana
pyruvate + NADH + H+ + CO2
-
-
-
ir
Subunits
Subunits
Commentary
Organism
dimer
isozymes NAD-ME1 and NAD-ME2 assemble as homo- and heterodimers, the latter is termed NAD-MEH, in vitro and in vivo. Interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour; isozymes NAD-ME1 and NAD-ME2 assemble as homo- and heterodimers, the latter is termed NAD-MEH, in vitro and in vivo. Interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour
Arabidopsis thaliana
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
46
-
NAD+
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
46
-
(S)-malate
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
forward reaction, assay at; forward reaction, assay at
Arabidopsis thaliana
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
;
Arabidopsis thaliana
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.041
-
NADH
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
0.15
-
NADH
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
0.45
-
5'-AMP
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
0.8
-
Tartrate
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
1.5
-
5'-AMP
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
3
-
CO2
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
4
-
Tartrate
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
7
-
CO2
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
11
-
pyruvate
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
14
-
pyruvate
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of NAD-ME1, NAD-ME2, and NAD-MEH
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Arabidopsis thaliana
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of a chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, NAD-ME1q shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
Arabidopsis thaliana
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(S)-malate
isozyme NAD-ME2, competitive
Arabidopsis thaliana
5'-AMP
isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate
Arabidopsis thaliana
CO2
isozyme NAD-ME2 and chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate
Arabidopsis thaliana
CO2
chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate
Arabidopsis thaliana
additional information
product inhibition patterns of isozyme NAD-ME2, overview
Arabidopsis thaliana
NADH
isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate. NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q
Arabidopsis thaliana
NADH
NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q
Arabidopsis thaliana
pyruvate
isozyme NAD-ME2, uncompetitive versus NAD+, mixed inhibition versus (S)-malate. Pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q
Arabidopsis thaliana
pyruvate
pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q
Arabidopsis thaliana
Tartrate
substrate analogue, isozyme NAD-ME2, uncompetitive versus NAD+, competitive versus (S)-malate
Arabidopsis thaliana
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.041
-
NADH
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
0.15
-
NADH
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
0.45
-
5'-AMP
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
0.8
-
Tartrate
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
1.5
-
5'-AMP
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
3
-
CO2
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
4
-
Tartrate
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
7
-
CO2
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
11
-
pyruvate
versus NAD+, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
14
-
pyruvate
versus (S)-malate, pH 6.5, temperature not specified in the publication, isozyme NAD-ME2
Arabidopsis thaliana
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Isozyme NAD-ME2 follows a sequential ordered Bi-Ter mechanism. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
Arabidopsis thaliana
additional information
-
additional information
kinetic mechanisms of homodimers NAD-ME1 and NAD-ME2, and of NAD-ME heterodimer NAD-MEH, overview. The first 176 amino acids are associated with the differences observed in the kinetic mechanisms of the enzymes. Activity of NAD-ME1 in the direction of malate decarboxylation shows a hyperbolic response, proposed kinetic model for NAD-ME1. Kinetic properties and mechanism of chimeric mutant NAD-ME1q, overview
Arabidopsis thaliana
1.1
-
NAD+
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
2.6
-
(S)-malate
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
isozymes NAD-ME1 and NAD-ME2
Arabidopsis thaliana
5739
-
mitochondrion
isozyme NAD-ME1
Arabidopsis thaliana
5739
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mn2+
activates probably
Arabidopsis thaliana
Mn2+
activates
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Arabidopsis thaliana
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
pyruvate + NADH + H+ + CO2
-
-
r
(S)-malate + NAD+
Arabidopsis thaliana
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
pyruvate + NADH + H+ + CO2
-
-
ir
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant NAD-ME1, NAD-ME2, and NAD-MEH
Arabidopsis thaliana
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
711147
Arabidopsis thaliana
pyruvate + NADH + H+ + CO2
-
-
-
r
(S)-malate + NAD+
NAD-ME1, -ME2 and -MEH catalyse the reverse reaction of pyruvate reductive carboxylation with very low catalytic activity, supporting the notion that these isoforms act only in (S)-malate oxidation in plant mitochondria
711147
Arabidopsis thaliana
pyruvate + NADH + H+ + CO2
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
isozymes NAD-ME1 and NAD-ME2 assemble as homo- and heterodimers, the latter is termed NAD-MEH, in vitro and in vivo. Interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour
Arabidopsis thaliana
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
46
-
NAD+
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
46
-
(S)-malate
isozyme NAD-ME2, pH 6.5, temperature not specified in the publication
Arabidopsis thaliana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.5
-
forward reaction, assay at
Arabidopsis thaliana
General Information
General Information
Commentary
Organism
additional information
interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism; interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
Arabidopsis thaliana
physiological function
for a metabolic condition in which the mitochondrial NAD level is low and the (S)-malate level is high, the activity of homodimeric isozyme NAD-ME2 and/or heterodimer NAD-MEH would be preferred over that of homodimeric isozyme NAD-ME1; for a metabolic condition in which the mitochondrial NAD level is low and the (S)-malate level is high, the activity of homodimeric isozyme NAD-ME2 and/or heterodimer NAD-MEH would be preferred over that of homodimeric isozyme NAD-ME1
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
additional information
interaction between NAD-ME1 and -ME2 generates a heteromeric enzyme NAD-MEH with a particular kinetic behaviour. The N-terminal region of NAD-ME1 and -ME2 is associated with the order of substrate binding. The chimeric enzyme NAD-ME1q, that is composed of the first 176 amino acid residues of NAD-ME2 and the central and C-terminal sequence of NAD-ME1, shows a hyperbolic behaviour for (S)-malate and NAD+. Product-inhibition pattern of NAD-ME1q with the three products supports a sequential ordered mechanism
Arabidopsis thaliana
physiological function
for a metabolic condition in which the mitochondrial NAD level is low and the (S)-malate level is high, the activity of homodimeric isozyme NAD-ME2 and/or heterodimer NAD-MEH would be preferred over that of homodimeric isozyme NAD-ME1
Arabidopsis thaliana
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
-
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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
-
-
-
-
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
-
-
-
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-
1
1
-
-
-
-
-
-
2
-
1
-
2
-
-
-
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-
-
-
-
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
-
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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
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
-
-
-
1
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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1
-
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-
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-
-
1
-
1
-
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-
-
1
-
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1
-
-
-
-
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286704
Day
Activation of NAD-linked malic ...
Brassica oleracea, Solanum tuberosum
Arch. Biochem. Biophys.
231
233-242
1984
2
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2
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2
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2
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4
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286705
Canellas
Kinetic properties of NAD mali ...
Brassica oleracea
Arch. Biochem. Biophys.
229
414-425
1984
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2
3
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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
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1
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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
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2
4
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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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6
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7
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4
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1
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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
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1
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1
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286709
Wedding
Slow transients in the activit ...
Crassula argentea
Plant Physiol.
68
1416-1423
1981
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-
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2
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1
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1
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1
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1
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1
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1
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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
-
2
3
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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
3
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2
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8
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2
3
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1
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1
1
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2
1
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1
3
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-
-
-
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-
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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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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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2
2
2
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11
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1
1
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12
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1
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12
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12
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2
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1
1
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12
-
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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
4
1
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6
1
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4
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1
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1
4
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2
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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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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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2
8
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
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2
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