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show all sequences of 1.1.1.38

Structural characteristics of the nonallosteric human cytosolic malic enzyme

Hsieh, J.; Li, S.; Chen, M.; Yang, P.; Chen, H.; Chan, N.; Liu, J.; Hung, H.; Biochim. Biophys. Acta 1844, 1773-1783 (2014)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
fumarate
mitochondrial NAD(P)+-dependent malic enzyme (m-NAD(P)-ME) is allosterically activated by fumarate
Homo sapiens
additional information
cytosolic NADP+-dependent malic enzyme (c-NADP-ME) is neither a cooperative nor an allosteric enzyme
Homo sapiens
Cloned(Commentary)
Commentary
Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
K57S/E59N/K73E/D102S
site-directed mutagenesis
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
cytosolic NADP+-dependent malic enzyme (c-NADP-ME) is neither a cooperative nor an allosteric enzyme
Homo sapiens
0.3
-
NADH
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S; pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with 5 mM fumarate; pH 7.4, 30°C, recombinant wild-type with 5 mM fumarate
Homo sapiens
1.4
-
NADH
pH 7.4, 30°C, recombinant wild-type
Homo sapiens
3
-
(S)-malate
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S
Homo sapiens
3.6
-
(S)-malate
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with 5 mM fumarate
Homo sapiens
4.6
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme with 5 mM fumarate
Homo sapiens
15.6
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Homo sapiens
5829
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Homo sapiens
-
pyruvate + CO2 + NADH
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P23368
-
-
Purification (Commentary)
Commentary
Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
-
737754
Homo sapiens
pyruvate + CO2 + NADH
-
-
-
r
Subunits
Subunits
Commentary
Organism
dimer and tetramer
-
Homo sapiens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Homo sapiens
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5
-
(S)-malate
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with or without 5 mM fumarate
Homo sapiens
43
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme
Homo sapiens
55
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme with 5 mM fumarate
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the isoenzyme can also use NADP+ but is more effective with NAD+
Homo sapiens
NAD+
-
Homo sapiens
NADH
-
Homo sapiens
NADP+
-
Homo sapiens
NADPH
-
Homo sapiens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
fumarate
mitochondrial NAD(P)+-dependent malic enzyme (m-NAD(P)-ME) is allosterically activated by fumarate
Homo sapiens
additional information
cytosolic NADP+-dependent malic enzyme (c-NADP-ME) is neither a cooperative nor an allosteric enzyme
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the isoenzyme can also use NADP+ but is more effective with NAD+
Homo sapiens
NAD+
-
Homo sapiens
NADH
-
Homo sapiens
NADP+
-
Homo sapiens
NADPH
-
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K57S/E59N/K73E/D102S
site-directed mutagenesis
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
cytosolic NADP+-dependent malic enzyme (c-NADP-ME) is neither a cooperative nor an allosteric enzyme
Homo sapiens
0.3
-
NADH
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S; pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with 5 mM fumarate; pH 7.4, 30°C, recombinant wild-type with 5 mM fumarate
Homo sapiens
1.4
-
NADH
pH 7.4, 30°C, recombinant wild-type
Homo sapiens
3
-
(S)-malate
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S
Homo sapiens
3.6
-
(S)-malate
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with 5 mM fumarate
Homo sapiens
4.6
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme with 5 mM fumarate
Homo sapiens
15.6
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Homo sapiens
5829
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(S)-malate + NAD+
Homo sapiens
-
pyruvate + CO2 + NADH
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-malate + NAD+
-
737754
Homo sapiens
pyruvate + CO2 + NADH
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
dimer and tetramer
-
Homo sapiens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Homo sapiens
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5
-
(S)-malate
pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with or without 5 mM fumarate
Homo sapiens
43
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme
Homo sapiens
55
-
(S)-malate
pH 7.4, 30°C, recombinant wild-type enzyme with 5 mM fumarate
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.4
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
additional information
the molecular basis for the different allosteric properties and quaternary structural stability of m-NAD(P)-ME, EC 1.1.1.38 and c-NADP-ME, EC 1.1.1.40. The structural features near the fumarate binding site and the dimer interface are highly related to the quaternary structural stability of c-NADP-ME and m-NAD(P)-ME. Lys57 plays functional roles in both the allosteric regulation and the subunit-subunit interaction of humanm-NAD(P)-ME
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
additional information
the molecular basis for the different allosteric properties and quaternary structural stability of m-NAD(P)-ME, EC 1.1.1.38 and c-NADP-ME, EC 1.1.1.40. The structural features near the fumarate binding site and the dimer interface are highly related to the quaternary structural stability of c-NADP-ME and m-NAD(P)-ME. Lys57 plays functional roles in both the allosteric regulation and the subunit-subunit interaction of humanm-NAD(P)-ME
Homo sapiens
Other publictions for EC 1.1.1.38
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)
741010
Hasan
Mitochondrial malic enzyme 3 i ...
Rattus norvegicus
Mol. Endocrinol.
29
396-410
2015
-
-
1
-
1
-
-
-
1
-
-
2
-
1
-
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-
-
-
3
-
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2
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1
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4
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1
4
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1
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1
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2
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-
-
3
-
-
2
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1
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-
1
1
-
-
-
737754
Hsieh
Structural characteristics of ...
Homo sapiens
Biochim. Biophys. Acta
1844
1773-1783
2014
2
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1
-
1
-
-
7
3
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1
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2
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1
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1
1
1
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1
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5
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1
5
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1
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7
3
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1
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1
1
1
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3
1
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1
1
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-
721800
Hou
Efficient synthesis of triazol ...
Escherichia coli
Bioorg. Med. Chem. Lett.
21
1667-1669
2011
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12
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1
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12
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1
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1
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1
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-
-
-
-
695884
MacDonald
Mitochondrial malic enzyme (ME ...
Homo sapiens, Mus musculus, Rattus norvegicus
Arch. Biochem. Biophys.
488
100-104
2009
3
-
-
-
-
-
3
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3
-
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3
-
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7
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3
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3
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3
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3
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3
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3
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7
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
699052
Zheng
Production of L-malic acid wit ...
Brevundimonas diminuta, Brevundimonas diminuta IFO13182
J. Biosci. Bioeng.
107
16-20
2009
-
-
-
-
-
-
-
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4
-
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1
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2
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1
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2
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-
-
-
-
-
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-
-
-
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-
685215
Aktas
Proper positioning of the nico ...
Ascaris suum
Biochemistry
47
2539-2546
2008
-
-
-
-
4
-
-
-
1
-
-
-
-
2
-
-
-
-
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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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-
-
-
-
-
-
-
689861
Wang
Over-expression, purification, ...
Escherichia coli K-12
Protein Expr. Purif.
53
97-103
2007
-
-
1
-
-
-
-
2
-
1
3
1
-
4
-
-
1
-
-
-
-
-
1
1
1
-
-
1
1
1
-
1
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-
1
1
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-
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-
-
-
2
-
1
3
1
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-
-
1
-
-
-
-
1
1
1
-
-
1
1
1
-
-
-
-
-
-
-
-
656983
Lara
Induction of a crassulacean ac ...
Portulaca oleracea
Plant Cell Physiol.
45
618-626
2004
-
-
-
-
-
-
1
-
3
1
-
1
-
3
-
-
-
-
-
2
3
-
2
-
1
-
-
-
1
-
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1
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1
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1
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3
1
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1
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-
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2
3
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
656977
Sawada
Photosynthesis with single-roo ...
Amaranthus hybridus subsp. cruentus
Plant Cell Physiol.
43
1293-1301
2002
-
-
-
-
-
-
1
-
-
-
-
1
-
3
-
-
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-
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1
2
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2
-
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
2
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
286680
Viljoen
Mutation of Gly-444 inactivate ...
Schizosaccharomyces pombe
FEMS Microbiol. Lett.
167
157-162
1998
-
-
-
-
1
-
-
-
-
-
-
2
-
2
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3
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1
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1
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1
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3
-
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-
-
-
-
-
-
-
-
-
-
-
286677
Driscoll
Properties of NAD+ and NADP+-d ...
Sinorhizobium meliloti
Microbiology
143
489-498
1997
1
-
1
-
-
-
4
2
-
5
-
3
-
3
-
-
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1
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4
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1
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2
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1
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1
2
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4
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5
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3
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1
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4
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1
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286678
Chooback
Expression, purification, and ...
Ascaris suum
Protein Expr. Purif.
10
51-54
1997
-
-
1
-
-
-
-
4
1
-
-
2
-
4
-
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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
1
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4
1
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2
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1
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1
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
286679
Srivatava
-
Effect of silver nitrate on ac ...
Mangifera indica
Indian J. Exp. Biol.
34
575-576
1996
-
-
-
-
-
-
1
-
-
-
-
2
-
1
-
-
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-
-
-
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3
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1
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1
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1
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2
-
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-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286681
Karsten
Stepwise versus concerted oxid ...
Ascaris suum
Biochemistry
33
2096-2103
1994
-
-
-
-
-
-
-
-
1
-
-
2
-
3
-
-
1
1
-
-
1
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
-
1
-
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1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286682
Driscoll
NAD+-dependent malic enzyme of ...
Sinorhizobium meliloti
Mol. Microbiol.
7
865-873
1993
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
1
-
-
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-
-
-
1
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-
2
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286683
Furbank
Regulation of C4 photosynthesi ...
Atriplex spongiosa, Panicum miliaceum, Urochloa panicoides
Arch. Biochem. Biophys.
289
376-381
1991
4
-
-
-
-
-
10
-
-
-
-
6
-
6
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
3
-
-
-
4
-
-
3
-
-
-
-
10
-
-
-
-
-
6
-
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9
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286685
Park
pH Dependence of kinetic param ...
Ascaris suum
Biochemistry
25
3752-3759
1986
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3
-
3
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2
1
1
5
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4
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1
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1
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1
1
5
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4
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286684
Rao
Diethylpyrocarbonate inactivat ...
Ascaris suum
Arch. Biochem. Biophys.
241
67-74
1985
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286686
Park
Kinetic mechanism in the direc ...
Ascaris suum
Biochemistry
23
5446-5453
1984
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2
4
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2
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286687
Kiick
Determination of dissociation ...
Ascaris suum
Biochemistry
23
5454-5459
1984
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5
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2
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2
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1
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286688
Cook
Distinct metal cofactor-induce ...
Escherichia coli
Biochim. Biophys. Acta
749
198-203
1983
1
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3
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3
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286689
Yamaguchi
Studies on regulatory function ...
Escherichia coli
J. Biochem.
86
325-333
1979
3
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4
5
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4
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3
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7
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1
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1
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4
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2
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7
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2
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286690
Milne
-
Role of metal cofactors in enz ...
Escherichia coli
Biochemistry
18
3605-3610
1979
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2
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2
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2
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1
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3
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1
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1
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2
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3
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1
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286691
Rhathnam
-
Studies with isolated bundle s ...
Digitaria sanguinalis, Eleusine indica, Eriochloa borumensis, Megathyrsus maximus, Panicum miliaceum, Zea mays
FEBS Lett.
96
367-372
1978
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12
6
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12
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6
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18
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6
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6
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6
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12
6
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12
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18
-
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6
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286692
Iwakura
Studies on regulatory function ...
Agrobacterium tumefaciens, Citrobacter freundii, Clostridium tetanomorphum, Erwinia aroidea, Escherichia coli B, Escherichia coli K-12, Escherichia coli W, Klebsiella aerogenes, Klebsiella aerogenes IFO 3320, Proteus vulgaris
J. Biochem.
83
1387-1394
1978
6
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5
8
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11
20
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17
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10
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30
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9
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6
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9
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8
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11
20
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10
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30
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286693
Landsperger
NAD+-malic enzyme. Regulatory ...
Ascaris suum
J. Biol. Chem.
251
3599-3602
1976
1
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4
1
1
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1
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3
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286694
Yamaguchi
Studies on the regulatory func ...
Escherichia coli W
J. Biochem.
76
1259-1268
1974
4
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1
9
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2
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3
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1
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286695
Schutz
Das 'Malatenzym' von Lactobaci ...
Lactobacillus plantarum, Lactobacillus plantarum B38, Leuconostoc mesenteroides
Arch. Mikrobiol.
91
183-202
1973
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286696
Fuck
-pfelsäurestoffwechsel bei Sa ...
Saccharomyces cerevisiae
Arch. Mikrobiol.
89
223-231
1973
1
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286697
Yamaguchi M.; Tokushige
Studies on regulatory function ...
Escherichia coli W
J. Biochem.
73
169-180
1973
1
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7
5
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5
2
2
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1
1
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5
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2
2
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3
5
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1
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286698
Sauer
An NAD- and NADP-dependent mal ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
50
524-531
1973
1
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1
3
1
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286699
Kaufman
Biosynthesis of dicarboxylic a ...
Lactobacillus plantarum
J. Biol. Chem.
192
301-312
1951
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