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show all sequences of 1.1.1.82

Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix

Kawakami, R.; Sakuraba, H.; Goda, S.; Tsuge, H.; Ohshima, T.; Biochim. Biophys. Acta 1794, 1496-1504 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of MDH in Escherichia coli strain BL21(DE3) in inclusion bodies
Aeropyrum pernix
Crystallization (Commentary)
Crystallization
Organism
purified refolded reconbinant enzyme, sitting drop vapor diffusion method, 0.002 ml of protein solution containing 8.9 mg/ml protein in 50 mM Tris-HCl, pH7.5, containing 0.2 M NaCl, are mixed with an equal volume of the reservoir solution, comprised of 0.1 M CHES, pH 9.5, and 40% PEG 600, and equilibrated against 0.15 ml of reservoir solution at 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.9 A resolution and room temperature
Aeropyrum pernix
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.019
-
(S)-malate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
0.12
-
(S)-malate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
0.2
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
1.2
-
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
2
3
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
5.8
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33489
-
4 * 34000, recombinant enzyme, SDS-PAGE, 4 * 33489, sequence calculation
Aeropyrum pernix
34000
-
4 * 34000, recombinant enzyme, SDS-PAGE, 4 * 33489, sequence calculation
Aeropyrum pernix
110000
-
recombinant enzyme, gel filtration
Aeropyrum pernix
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Aeropyrum pernix
Q9YEA1
a strict aerobic hyperthermophilic archaeon isolated from a coastal thermal vent in Japan
-
Purification (Commentary)
Commentary
Organism
recombinant MDH from Escherichia coli inclusion bodies by solubilization, refolding, dialysis, and gel filtration
Aeropyrum pernix
Renatured (Commentary)
Commentary
Organism
solubilization and refolding of recombinant MDH from Escherichia coli inclusion bodies, the enzyme is dissolved in 6 M guanidine-HCl and gradually refolded to the active enzyme through dilution of the denaturant, conditions: refolding buffer 1.5 L of 0.1 M Tris-HCl, pH 7.5, containing 2 mM EDTA and 0.4 M L-arginine, incubation for 36 h at 4°C
Aeropyrum pernix
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S,3R)-tartrate + NAD(P)+
-
696461
Aeropyrum pernix
? + NAD(P)H + H+
-
-
-
?
(2S,3S)-tartrate + NAD(P)+
-
696461
Aeropyrum pernix
? + NAD(P)H + H+
-
-
-
?
(S)-malate + NAD(P)+
-
696461
Aeropyrum pernix
oxaloacetate + NAD(P)H + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
structure qand sequence comaprsion, overall structure, overview
Aeropyrum pernix
tetramer
4 * 34000, recombinant enzyme, SDS-PAGE, 4 * 33489, sequence calculation
Aeropyrum pernix
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
95
-
above
Aeropyrum pernix
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
50
95
-
Aeropyrum pernix
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
purified recombinant enzyme, 30 min, pH 5.0-10.5, stable
Aeropyrum pernix
90
-
purified recombinant enzyme, 10 min, stable. The hyperthermostability of the Aeropyrum pernix MDH is likely attributable to its smaller cavity volume and larger numbers of ion pairs and ion-pair networks, but the molecular strategy for thermostability may be specific for each enzyme
Aeropyrum pernix
100
-
purified recombinant enzyme, 10 min, stable. The hyperthermostability of the Aeropyrum pernix MDH is likely attributable to its smaller cavity volume and larger numbers of ion pairs and ion-pair networks, but the molecular strategy for thermostability may be specific for each enzyme
Aeropyrum pernix
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.16
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
0.2
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
0.37
-
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
1.4
-
(S)-malate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
2.6
-
(S)-malate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
4.1
-
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
11
-
-
Aeropyrum pernix
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
5
10.5
purified recombinant enzyme, 30 min, 50°C, stable
Aeropyrum pernix
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
NADP+ is the preferred cofactor compared to NAD+ with substrate (S)-malate, while NAD+ is preferred with substrate tartrate. Ala at position 53 is responsible for coenzyme specificity, and the next residue, Arg, is important for NADP+ binding, structural analysis and comparison
Aeropyrum pernix
NADP+
NADP+ is the preferred cofactor compared to NAD+ with substrate (S)-malate, while NAD+ is preferred with substrate tartrate. Ala at position 53 is responsible for coenzyme specificity, and the next residue, Arg, is important for NADP+ binding, structural analysis and comparison
Aeropyrum pernix
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of MDH in Escherichia coli strain BL21(DE3) in inclusion bodies
Aeropyrum pernix
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
NADP+ is the preferred cofactor compared to NAD+ with substrate (S)-malate, while NAD+ is preferred with substrate tartrate. Ala at position 53 is responsible for coenzyme specificity, and the next residue, Arg, is important for NADP+ binding, structural analysis and comparison
Aeropyrum pernix
NADP+
NADP+ is the preferred cofactor compared to NAD+ with substrate (S)-malate, while NAD+ is preferred with substrate tartrate. Ala at position 53 is responsible for coenzyme specificity, and the next residue, Arg, is important for NADP+ binding, structural analysis and comparison
Aeropyrum pernix
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified refolded reconbinant enzyme, sitting drop vapor diffusion method, 0.002 ml of protein solution containing 8.9 mg/ml protein in 50 mM Tris-HCl, pH7.5, containing 0.2 M NaCl, are mixed with an equal volume of the reservoir solution, comprised of 0.1 M CHES, pH 9.5, and 40% PEG 600, and equilibrated against 0.15 ml of reservoir solution at 20°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.9 A resolution and room temperature
Aeropyrum pernix
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.019
-
(S)-malate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
0.12
-
(S)-malate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
0.2
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
1.2
-
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
2
3
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
5.8
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33489
-
4 * 34000, recombinant enzyme, SDS-PAGE, 4 * 33489, sequence calculation
Aeropyrum pernix
34000
-
4 * 34000, recombinant enzyme, SDS-PAGE, 4 * 33489, sequence calculation
Aeropyrum pernix
110000
-
recombinant enzyme, gel filtration
Aeropyrum pernix
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant MDH from Escherichia coli inclusion bodies by solubilization, refolding, dialysis, and gel filtration
Aeropyrum pernix
Renatured (Commentary) (protein specific)
Commentary
Organism
solubilization and refolding of recombinant MDH from Escherichia coli inclusion bodies, the enzyme is dissolved in 6 M guanidine-HCl and gradually refolded to the active enzyme through dilution of the denaturant, conditions: refolding buffer 1.5 L of 0.1 M Tris-HCl, pH 7.5, containing 2 mM EDTA and 0.4 M L-arginine, incubation for 36 h at 4°C
Aeropyrum pernix
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(2S,3R)-tartrate + NAD(P)+
-
696461
Aeropyrum pernix
? + NAD(P)H + H+
-
-
-
?
(2S,3S)-tartrate + NAD(P)+
-
696461
Aeropyrum pernix
? + NAD(P)H + H+
-
-
-
?
(S)-malate + NAD(P)+
-
696461
Aeropyrum pernix
oxaloacetate + NAD(P)H + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
structure qand sequence comaprsion, overall structure, overview
Aeropyrum pernix
tetramer
4 * 34000, recombinant enzyme, SDS-PAGE, 4 * 33489, sequence calculation
Aeropyrum pernix
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
95
-
above
Aeropyrum pernix
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
50
95
-
Aeropyrum pernix
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
purified recombinant enzyme, 30 min, pH 5.0-10.5, stable
Aeropyrum pernix
90
-
purified recombinant enzyme, 10 min, stable. The hyperthermostability of the Aeropyrum pernix MDH is likely attributable to its smaller cavity volume and larger numbers of ion pairs and ion-pair networks, but the molecular strategy for thermostability may be specific for each enzyme
Aeropyrum pernix
100
-
purified recombinant enzyme, 10 min, stable. The hyperthermostability of the Aeropyrum pernix MDH is likely attributable to its smaller cavity volume and larger numbers of ion pairs and ion-pair networks, but the molecular strategy for thermostability may be specific for each enzyme
Aeropyrum pernix
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.16
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
0.2
-
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
0.37
-
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
1.4
-
(S)-malate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
2.6
-
(S)-malate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
Aeropyrum pernix
4.1
-
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
Aeropyrum pernix
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
11
-
-
Aeropyrum pernix
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
5
10.5
purified recombinant enzyme, 30 min, 50°C, stable
Aeropyrum pernix
Other publictions for EC 1.1.1.82
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)
735713
Dulermo
Analysis of ATP-citrate lyase ...
no activity in Yarrowia lipolytica
Biochim. Biophys. Acta
1851
1107-1117
2015
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1
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739249
Heyno
Putative role of the malate va ...
Arabidopsis thaliana
Philos. Trans. R. Soc. Lond. B Biol. Sci.
369
20130228
2014
1
-
-
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-
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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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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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723892
Libik-Konieczny
-
Pathogen-induced changes in ma ...
Mesembryanthemum crystallinum
Acta Physiol. Plant.
34
1471-1477
2012
-
1
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-
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1
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2
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-
2
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-
696461
Kawakami
Refolding, characterization an ...
Aeropyrum pernix
Biochim. Biophys. Acta
1794
1496-1504
2009
-
-
1
1
-
-
-
6
-
-
3
-
-
1
-
-
1
-
1
-
-
-
3
2
1
1
3
6
1
-
1
2
-
-
-
-
-
1
2
1
-
-
-
-
-
6
-
-
3
-
-
-
-
1
1
-
-
-
3
2
1
1
3
6
1
-
1
-
-
-
-
-
-
-
689663
Anderson
Distribution of thioredoxins f ...
Pisum sativum
Plant Sci.
174
432-445
2008
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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682850
Zhang
-
Characteristics of ribulose-1, ...
Oryza sativa
S. Afr. J. Bot.
73
22-28
2007
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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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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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1
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-
-
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-
688456
Hameister
Transcriptional regulation of ...
Arabidopsis lyrata subsp. petraea, Arabidopsis thaliana, Capsella bursa-pastoris, Capsella rubella, Cochlearia officinalis, Lepidium densiflorum, Lepidium latifolium
J. Mol. Evol.
65
437-455
2007
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7
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11
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7
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7
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7
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667200
Rondeau
NADP-malate dehydrogenase gene ...
Chrysopogon zizanioides, Dichanthium aristatum, Flaveria trinervia, Heteropogon contortus, Hyparrhenia rufa, Ischaemum koleostachys, Megathyrsus maximus, Melinis repens, Oplismenus compositus, Oryza sativa, Paspalidium geminatum, Paspalum paniculatum, Pogonatherum paniceum, Saccharum hybrid cultivar R570, Saccharum officinarum, Saccharum spontaneum, Sorghum arundinaceum, Sorghum bicolor, Themeda quadrivalvis, Zea mays
Ann. Bot.
96
1307-1314
2005
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31
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23
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23
-
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-
-
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-
670586
Lemaire
NADP-malate dehydrogenase from ...
Chlamydomonas reinhardtii
Plant Physiol.
137
514-521
2005
1
-
-
-
-
-
-
-
2
-
-
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5
-
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1
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657015
Gomez
NADP-malate dehydrogenase from ...
Chlamydomonas reinhardtii
Plant Mol. Biol.
48
211-221
2002
2
-
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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1
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287424
Schepens
The dimer contact area of sorg ...
Sorghum sp.
FEBS Lett.
471
240-244
2000
1
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3
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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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3
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1
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1
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1
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287425
Hirasawa
Oxidation-reduction properties ...
Sorghum bicolor, Sorghum sp.
Biochemistry
39
3344-3350
2000
2
-
-
-
2
-
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287395
Krimm
Direct NMR observation of the ...
Sorghum bicolor
J. Biol. Chem.
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1999
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287414
Johansson
Structural basis for light act ...
Sorghum bicolor
Biochemistry
38
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1999
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287423
Carr
Chloroplast NADP-malate dehydr ...
Flaveria bidentis
Structure
7
461-475
1999
1
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1
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287415
MacPherson
Crystallization and preliminar ...
Flaveria bidentis
Acta Crystallogr. Sect. D
54
654-656
1998
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1
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287422
Ruelland
The autoinhibition of sorghum ...
Sorghum sp.
J. Biol. Chem.
273
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1998
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287419
Riessland
Determination of the regulator ...
Pisum sativum
Biol. Chem.
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1997
2
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287427
Braun
Kinetic evidence for protein c ...
Glycine max
Eur. J. Biochem.
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287428
Lemaire
The catalytic site of chloropl ...
Sorghum sp.
Eur. J. Biochem.
236
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1996
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9
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6
1
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287417
Scheibe
Analysis of biophysical differ ...
Pisum sativum, Spinacia oleracea
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300
635-640
1993
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287386
Agostino
Amino acid sequence and molecu ...
Zea mays
Plant Physiol.
98
1506-1510
1992
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2
1
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287418
Kampfenkel
Limited proteolysis of NADP-ma ...
Pisum sativum
Biochim. Biophys. Acta
1156
71-77
1992
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2
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287421
Issakidis
Site-directed mutagenesis reve ...
Sorghum sp.
J. Biol. Chem.
267
21577-21583
1992
2
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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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2
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1
1
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-
287426
Jacquot
Properties of recombinant NADP ...
Sorghum bicolor
Eur. J. Biochem.
199
47-51
1991
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1
1
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1
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287385
Luchetta
Structure and characterization ...
Sorghum bicolor
Gene
89
171-177
1990
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2
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287387
Vairinhos
-
Purification and molecular for ...
Echinochloa crus-galli
Plant Sci.
71
173-177
1990
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287388
Miginiac-Maslow
-
Regulation of corn leaf NADP-m ...
Pisum sativum, Spinacia oleracea, Zea mays
Biochim. Biophys. Acta
1017
273-279
1990
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3
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287389
Scheibe
Structural and catalytic prope ...
Pisum sativum
Eur. J. Biochem.
189
581-587
1990
1
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1
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287413
Cretin
Primary structure of sorghum m ...
Sorghum bicolor
Eur. J. Biochem.
192
299-303
1990
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287420
Gupta
-
Properties of NADP+-malate deh ...
Cicer arietinum
Plant Physiol. Biochem.
28
671-678
1990
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7
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287390
Cheng
Photosynthesis in Flaveria bro ...
Flaveria brownii
Plant Physiol.
87
867-873
1988
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287391
Migniac-Maslow
Effect of high light intensiti ...
Spinacia oleracea
Planta
173
468-473
1988
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1
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287392
Fickenscher
Limited proteolysis of inactiv ...
Pisum sativum
Arch. Biochem. Biophys.
260
771-779
1988
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6
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1
1
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287393
Kagawa
NADP-malate dehydrogenase from ...
Zea mays
Arch. Biochem. Biophys.
260
674-695
1988
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287394
Jawali
-
Presence of essential histidin ...
Zea mays
Phytochemistry
26
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1987
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287396
Scheibe
-
NADP-malate dehydrogenase acti ...
Spinacia oleracea
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124
103-110
1986
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287397
Jacquot
-
Further evidence for a role of ...
Zea mays
FEBS Lett.
209
87-91
1986
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287398
Nakamoto
Light activation of pyruvate, ...
Zea mays
Plant Physiol.
82
312-315
1986
1
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287400
Scheibe
-
Studies on the mechanism of th ...
Pisum sativum
Biochim. Biophys. Acta
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191-197
1986
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287401
Ferte
Structural, immunological and ...
Spinacia oleracea, Zea mays
Eur. J. Biochem.
154
587-595
1986
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2
2
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287399
Edwards
-
Pyruvate, Pi dikinase and NADP ...
Pisum sativum, Zea mays
Annu. Rev. Plant Physiol.
36
255-286
1985
2
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2
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2
2
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1
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287402
Gotow
Light activation of NADP-malat ...
Vicia faba
Plant Physiol.
79
829-832
1985
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287405
Scheibe
-
The dark (oxidized) form of th ...
Pisum sativum
FEBS Lett.
180
317-320
1985
1
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2
6
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6
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286653
Isegawa
-
Submitochondrial location and ...
Euglena gracilis, Euglena gracilis SM-ZK
Agric. Biol. Chem.
48
549-552
1984
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8
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2
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1
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1
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287403
Ferte
-
Purification of several NADP-d ...
Spinacia oleracea
Plant Sci. Lett.
37
115-121
1984
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4
2
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1
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287406
Perrot-Rechenmann
-
Localization of NADP-malate de ...
Zea mays
Plant Sci. Lett.
30
219-226
1983
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1
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1
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287407
Scheibe
NADP regulates the light activ ...
Pisum sativum
Planta
157
548-553
1983
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1
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1
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287409
Fickenscher
-
Purification and properties of ...
Pisum sativum
Biochim. Biophys. Acta
749
249-254
1983
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4
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4
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1
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4
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4
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1
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1
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2
4
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287410
Ferte
-
Molecular properties and thior ...
Spinacia oleracea
FEBS Lett.
146
133-138
1982
1
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1
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1
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287411
Jacquot
Enzyme regulation in C4 photos ...
Zea mays
Plant Physiol.
68
300-304
1981
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1
1
2
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1
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287412
Mohamed
Extraction of chloroplast ligh ...
Pisum sativum
Arch. Biochem. Biophys.
209
606-612
1981
1
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287404
Wolosiuk
-
Regulation of NADP-malate dehy ...
Spinacia oleracea
FEBS Lett.
81
253-258
1977
1
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1
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1
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287384
Johnson
NADP-malate dehydrogenase: pho ...
Hordeum vulgare, Spinacia oleracea
Biochem. Biophys. Res. Commun.
43
703-709
1971
2
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4
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2
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1
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4
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287416
Hatch
NADPH-specific malate dehydrog ...
Amaranthus palmeri, Beta vulgaris, Daucus carota, Pisum sativum, Saccharum sp., Spinacia oleracea, Zea mays
Biochem. Biophys. Res. Commun.
34
589-593
1969
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3
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3
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5
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7
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3
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15
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1
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3
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3
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5
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3
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15
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1
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