BRENDA - Enzyme Database show
show all sequences of 1.1.1.93

Purification and characterization of a bifunctional L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) from Rhodopseudomonas sphaeroides Y

Giffhorn, F.; Kuhn, A.; J. Bacteriol. 155, 281-290 (1983)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
NH4+
monovalent and divalent cations are essential for optimal activity. At saturating concentrations of 0.4 mM MnCl2 ammonium sulfate stimulates optimally over a broad concentration range, from 40 mM to 100 mM
Rhodobacter sphaeroides
General Stability
General Stability
Organism
repeated freezing and thawing of purified enzyme, 10-40% loss of activity
Rhodobacter sphaeroides
Inhibitors
Inhibitors
Commentary
Organism
Structure
ATP
-
Rhodobacter sphaeroides
Dihydroxyfumarate
-
Rhodobacter sphaeroides
meso-tartrate
competitive
Rhodobacter sphaeroides
oxaloacetate
competitive
Rhodobacter sphaeroides
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.13
-
NAD+
reaction with D-malate
Rhodobacter sphaeroides
0.17
-
D-malate
-
Rhodobacter sphaeroides
0.28
-
NAD+
reaction with (+ L-(+)-tartrate)
Rhodobacter sphaeroides
2.3
-
L-Tartrate
-
Rhodobacter sphaeroides
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
1 mM, 30% of the activation with 0.4 mM MnCl2
Rhodobacter sphaeroides
K+
50 mM K2SO4, 56% of the activation with 50 mM KCl; 50 mM KCl, 63% of the activation with 50 mM NH4Cl
Rhodobacter sphaeroides
Mg2+
5 mM, 59% of the activation with 0.4 mM MnCl2
Rhodobacter sphaeroides
Mn2+
Km: 0.016 mM, reaction with L-malate or D-malate; monovalent and divalent cations are essential for optimal activity. At saturating concentrations of 0.4 mM MnCl2 ammonium sulfate stimulates optimally over a broad concentration range, from 40 mM to 100 mM
Rhodobacter sphaeroides
NaCl
50 mM KCl, 19% of the activation with 50 mM NH4Cl
Rhodobacter sphaeroides
Zn2+
0.1 mM, 14% of the activation with 0.4 mM MnCl2
Rhodobacter sphaeroides
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38500
-
4 * 38500, SDS-PAGE
Rhodobacter sphaeroides
158000
-
gel filtration
Rhodobacter sphaeroides
162000
-
ultracentrifugation
Rhodobacter sphaeroides
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter sphaeroides
-
-
-
Purification (Commentary)
Commentary
Organism
bifunctional L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating), EC 1.1.1.93/EC 1.1.1.83
Rhodobacter sphaeroides
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.88
-
-
Rhodobacter sphaeroides
Storage Stability
Storage Stability
Organism
-20C, months, partially purified enzyme
Rhodobacter sphaeroides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tartrate + NAD+
-
389609
Rhodobacter sphaeroides
oxaloglycolate + NADH + H+
dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
389609
Rhodobacter sphaeroides
?
L-tartrate + NAD+
-
389609
Rhodobacter sphaeroides Y
oxaloglycolate + NADH + H+
dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
389609
Rhodobacter sphaeroides Y
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 38500, SDS-PAGE
Rhodobacter sphaeroides
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
-
Rhodobacter sphaeroides
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
pH 7.0, 30 h: 50% loss of activity. pH 8.5, stable for 4 h
Rhodobacter sphaeroides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
9
bifunctional L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83
Rhodobacter sphaeroides
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
10.6
at pH 7.0 and pH 10.6: 50% of activity maximum
Rhodobacter sphaeroides
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
cofactor
Rhodobacter sphaeroides
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
NH4+
monovalent and divalent cations are essential for optimal activity. At saturating concentrations of 0.4 mM MnCl2 ammonium sulfate stimulates optimally over a broad concentration range, from 40 mM to 100 mM
Rhodobacter sphaeroides
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
cofactor
Rhodobacter sphaeroides
General Stability (protein specific)
General Stability
Organism
repeated freezing and thawing of purified enzyme, 10-40% loss of activity
Rhodobacter sphaeroides
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ATP
-
Rhodobacter sphaeroides
Dihydroxyfumarate
-
Rhodobacter sphaeroides
meso-tartrate
competitive
Rhodobacter sphaeroides
oxaloacetate
competitive
Rhodobacter sphaeroides
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.13
-
NAD+
reaction with D-malate
Rhodobacter sphaeroides
0.17
-
D-malate
-
Rhodobacter sphaeroides
0.28
-
NAD+
reaction with (+ L-(+)-tartrate)
Rhodobacter sphaeroides
2.3
-
L-Tartrate
-
Rhodobacter sphaeroides
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
1 mM, 30% of the activation with 0.4 mM MnCl2
Rhodobacter sphaeroides
K+
50 mM K2SO4, 56% of the activation with 50 mM KCl; 50 mM KCl, 63% of the activation with 50 mM NH4Cl
Rhodobacter sphaeroides
Mg2+
5 mM, 59% of the activation with 0.4 mM MnCl2
Rhodobacter sphaeroides
Mn2+
Km: 0.016 mM, reaction with L-malate or D-malate; monovalent and divalent cations are essential for optimal activity. At saturating concentrations of 0.4 mM MnCl2 ammonium sulfate stimulates optimally over a broad concentration range, from 40 mM to 100 mM
Rhodobacter sphaeroides
NaCl
50 mM KCl, 19% of the activation with 50 mM NH4Cl
Rhodobacter sphaeroides
Zn2+
0.1 mM, 14% of the activation with 0.4 mM MnCl2
Rhodobacter sphaeroides
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38500
-
4 * 38500, SDS-PAGE
Rhodobacter sphaeroides
158000
-
gel filtration
Rhodobacter sphaeroides
162000
-
ultracentrifugation
Rhodobacter sphaeroides
Purification (Commentary) (protein specific)
Commentary
Organism
bifunctional L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating), EC 1.1.1.93/EC 1.1.1.83
Rhodobacter sphaeroides
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
1.88
-
-
Rhodobacter sphaeroides
Storage Stability (protein specific)
Storage Stability
Organism
-20C, months, partially purified enzyme
Rhodobacter sphaeroides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-tartrate + NAD+
-
389609
Rhodobacter sphaeroides
oxaloglycolate + NADH + H+
dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
389609
Rhodobacter sphaeroides
?
L-tartrate + NAD+
-
389609
Rhodobacter sphaeroides Y
oxaloglycolate + NADH + H+
dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
389609
Rhodobacter sphaeroides Y
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 38500, SDS-PAGE
Rhodobacter sphaeroides
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
50
-
-
Rhodobacter sphaeroides
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
30
-
pH 7.0, 30 h: 50% loss of activity. pH 8.5, stable for 4 h
Rhodobacter sphaeroides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.4
9
bifunctional L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83
Rhodobacter sphaeroides
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
10.6
at pH 7.0 and pH 10.6: 50% of activity maximum
Rhodobacter sphaeroides
Other publictions for EC 1.1.1.93
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)
710720
Malik
Structural characterization of ...
Pseudomonas putida
Acta Crystallogr. Sect. D
66
673-684
2010
-
-
1
1
6
-
-
8
-
-
-
-
-
2
-
-
1
1
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
1
-
1
6
-
-
-
-
8
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
8
8
667741
Karsten
An isothermal titration calori ...
Pseudomonas putida
Biochemistry
45
9000-9006
2006
-
-
-
-
-
-
-
1
-
2
-
-
-
2
-
-
-
1
-
-
-
-
2
1
1
-
-
-
1
-
-
1
-
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1
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1
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2
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2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
654622
Karsten
Tartrate dehydrogenase catalyz ...
Escherichia coli
Biochemistry
41
12193-12199
2002
-
-
-
-
-
-
-
-
-
1
-
-
-
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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3
-
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-
-
1
-
-
-
-
-
-
-
-
389612
Tipton
-
Tartrate dehydrogenase, an enz ...
Pseudomonas putida
Protein Pept. Lett.
7
323-332
2000
1
-
-
-
-
-
3
4
-
4
-
1
-
1
-
-
-
1
-
-
-
-
5
-
-
-
-
4
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
3
-
4
-
4
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
389619
Tsukatani
-
Quantification of L-tartrate i ...
Escherichia coli
Anal. Sci.
16
265-268
2000
-
1
-
-
-
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
-
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-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
389613
Harve
Production and purification of ...
Pseudomonas putida
Appl. Biochem. Biotechnol.
70-72
677-686
1998
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
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-
-
1
-
-
-
-
-
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-
1
-
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-
-
-
-
1
-
-
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-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389614
Tipton
Transient-state kinetic analys ...
Pseudomonas putida
Biochemistry
35
3108-3114
1996
-
-
-
-
-
-
1
1
-
-
-
-
-
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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1
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1
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-
-
3
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
349359
Serfozo
Substrate determinants of the ...
Pseudomonas putida
Biochemistry
34
7517-7524
1995
-
-
-
-
-
-
-
14
-
-
-
-
-
1
-
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14
-
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1
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1
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14
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14
-
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-
-
-
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-
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349358
Beecher
Tartrate dehydrogenase-oxalate ...
Pseudomonas putida
Arch. Biochem. Biophys.
315
255-261
1994
-
-
-
-
-
-
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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-
389617
Tipton
Tartrate dehydrogenase, a new ...
Pseudomonas putida
Arch. Biochem. Biophys.
313
15-21
1994
-
-
1
-
-
-
-
3
-
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1
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3
-
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2
1
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3
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1
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1
1
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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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389618
Tipton
Characterization of the multip ...
Pseudomonas putida
Biochemistry
29
1749-1756
1990
-
-
-
-
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1
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-
2
2
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2
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1
1
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1
1
1
1
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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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1
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1
1
1
1
-
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-
-
-
-
-
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-
-
-
-
-
389611
Gifforn
-
L-(+)-Tartrate ...
Rhodobacter sphaeroides
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
7
78-85
1985
-
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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287429
Ebbighausen
-
A novel mechanism involved in ...
Rhodobacter sphaeroides
Arch. Microbiol.
138
338-344
1984
-
-
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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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-
389609
Giffhorn
Purification and characterizat ...
Rhodobacter sphaeroides
J. Bacteriol.
155
281-290
1983
1
-
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1
4
4
-
6
3
-
-
2
-
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1
-
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-
1
1
2
1
1
-
1
-
1
1
-
1
-
-
-
1
-
-
1
-
-
1
-
4
-
4
-
6
3
-
-
-
-
1
-
-
1
1
2
1
1
-
1
-
1
1
-
-
-
-
-
-
-
-
389610
Kohn
Tartaric acid metabolism. V. C ...
Pseudomonas putida
J. Biol. Chem.
243
2479-2485
1968
-
-
-
1
-
-
-
5
-
1
2
-
-
1
-
-
1
-
-
-
1
-
3
1
-
-
-
-
2
2
-
2
-
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-
-
2
1
-
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5
-
1
2
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1
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1
-
3
1
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-
2
2
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