BRENDA - Enzyme Database show
show all sequences of 1.1.1.93

Structural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactions

Malik, R.; Viola, R.E.; Acta Crystallogr. Sect. D 66, 673-684 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Pseudomonas putida
Crystallization (Commentary)
Crystallization
Organism
in complex with the intermediate analog oxalate, Mg2+ and NADH, to 2.0 A resolution
Pseudomonas putida
Engineering
Amino acid exchange
Commentary
Organism
D225A
mutation in metal ion-binding ligand, 20fold decrease in metal ion-binding affinity and a two-orders-of-magnitude decrease in catalysis
Pseudomonas putida
D250A
mutation in metal ion-binding ligand, 10fold decrease in metal ion-binding affinity and a two-orders-of-magnitude decrease in catalysis
Pseudomonas putida
R108L
1.3% of wild-type catalytic rate
Pseudomonas putida
R108Q
8.7% of wild-type catalytic rate
Pseudomonas putida
R98L
mutant is not expressed in stable form
Pseudomonas putida
R98Q
2.6% of wild-type catalytic rate
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.025
-
NAD+
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.079
-
D-malate
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.093
-
D-malate
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.096
-
NAD+
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.098
-
D-malate
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.135
-
NAD+
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.18
-
D-malate
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.24
-
NAD+
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas putida
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme
Pseudomonas putida
Reaction
Reaction
Commentary
Organism
tartrate + NAD+ = oxaloglycolate + NADH + H+
lysyl amino group, Lys192 is the base responsible for the water-mediated proton abstraction from the C2 hydroxyl group of the substrate that begins the catalytic reaction, followed by hydride transfer to NAD. The hydroxyl group of Tyr141 functions as a general acid to protonate the enolate intermediate. Each substrate undergoes the initial hydride transfer
Pseudomonas putida
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-malate + NAD+
-
710720
Pseudomonas putida
pyruvate + CO2 + NADH + H+
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.015
-
NAD+
mutant D225A, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.06
-
NAD+
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.087
-
NAD+
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.088
-
NAD+
mutant D250A, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.175
-
NAD+
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
6.5
-
NAD+
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Pseudomonas putida
Crystallization (Commentary) (protein specific)
Crystallization
Organism
in complex with the intermediate analog oxalate, Mg2+ and NADH, to 2.0 A resolution
Pseudomonas putida
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D225A
mutation in metal ion-binding ligand, 20fold decrease in metal ion-binding affinity and a two-orders-of-magnitude decrease in catalysis
Pseudomonas putida
D250A
mutation in metal ion-binding ligand, 10fold decrease in metal ion-binding affinity and a two-orders-of-magnitude decrease in catalysis
Pseudomonas putida
R108L
1.3% of wild-type catalytic rate
Pseudomonas putida
R108Q
8.7% of wild-type catalytic rate
Pseudomonas putida
R98L
mutant is not expressed in stable form
Pseudomonas putida
R98Q
2.6% of wild-type catalytic rate
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.025
-
NAD+
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.079
-
D-malate
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.093
-
D-malate
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.096
-
NAD+
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.098
-
D-malate
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.135
-
NAD+
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.18
-
D-malate
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.24
-
NAD+
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-malate + NAD+
-
710720
Pseudomonas putida
pyruvate + CO2 + NADH + H+
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.015
-
NAD+
mutant D225A, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.06
-
NAD+
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.087
-
NAD+
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.088
-
NAD+
mutant D250A, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.175
-
NAD+
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
6.5
-
NAD+
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.36
-
NAD+
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.48
-
D-malate
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
1.8
-
D-malate
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
1.8
-
NAD+
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
4.3
-
NAD+
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
6.2
-
D-malate
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
82
-
D-malate
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
260
-
NAD+
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.36
-
NAD+
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
0.48
-
D-malate
mutant R108L, pH 7.5, temperature not specified in the publication
Pseudomonas putida
1.8
-
D-malate
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
1.8
-
NAD+
mutant R98Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
4.3
-
NAD+
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
6.2
-
D-malate
mutant R108Q, pH 7.5, temperature not specified in the publication
Pseudomonas putida
82
-
D-malate
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
260
-
NAD+
wild-type, pH 7.5, temperature not specified in the publication
Pseudomonas putida
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
-
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1
1
6
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6
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6
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6
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8
8
667741
Karsten
An isothermal titration calori ...
Pseudomonas putida
Biochemistry
45
9000-9006
2006
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-
-
-
-
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1
-
2
-
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2
-
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1
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2
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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2
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2
1
1
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1
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654622
Karsten
Tartrate dehydrogenase catalyz ...
Escherichia coli
Biochemistry
41
12193-12199
2002
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1
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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
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-
-
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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
-
-
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-
3
-
4
-
4
-
1
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-
-
-
5
-
-
-
-
4
-
-
-
-
-
-
-
-
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389619
Tsukatani
-
Quantification of L-tartrate i ...
Escherichia coli
Anal. Sci.
16
265-268
2000
-
1
-
-
-
1
-
-
-
1
-
-
-
1
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-
1
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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
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-
1
-
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-
1
-
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-
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389613
Harve
Production and purification of ...
Pseudomonas putida
Appl. Biochem. Biotechnol.
70-72
677-686
1998
-
-
-
-
-
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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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1
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1
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1
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1
-
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-
-
-
-
-
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-
-
-
-
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
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349359
Serfozo
Substrate determinants of the ...
Pseudomonas putida
Biochemistry
34
7517-7524
1995
-
-
-
-
-
-
-
14
-
-
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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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349358
Beecher
Tartrate dehydrogenase-oxalate ...
Pseudomonas putida
Arch. Biochem. Biophys.
315
255-261
1994
-
-
-
-
-
-
1
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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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1
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389617
Tipton
Tartrate dehydrogenase, a new ...
Pseudomonas putida
Arch. Biochem. Biophys.
313
15-21
1994
-
-
1
-
-
-
-
3
-
-
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
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1
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1
1
1
1
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389611
Gifforn
-
L-(+)-Tartrate ...
Rhodobacter sphaeroides
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
7
78-85
1985
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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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389609
Giffhorn
Purification and characterizat ...
Rhodobacter sphaeroides
J. Bacteriol.
155
281-290
1983
1
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1
4
4
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6
3
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2
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1
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1
1
2
1
1
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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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1
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4
-
4
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6
3
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1
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1
1
2
1
1
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1
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1
1
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389610
Kohn
Tartaric acid metabolism. V. C ...
Pseudomonas putida
J. Biol. Chem.
243
2479-2485
1968
-
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1
-
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5
-
1
2
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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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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
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3
1
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2
2
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