BRENDA - Enzyme Database show
show all sequences of 1.3.1.7

Tartrate dehydrogenase-oxalate complexes: formation of a stable analog of a reaction intermediate complex

Beecher, B.S.; Koder, R.L.; Tipton, P.A.; Arch. Biochem. Biophys. 315, 255-261 (1994)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
Escherichia coli cells containing the plasmid pTDH1 which contains the gene encoding TDH under the control of the T7 polymerase promoter
Escherichia coli
Inhibitors
Inhibitors
Commentary
Organism
Structure
oxalate
time-dependent inhibition
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.032
-
D-malate
thio-NAD+ as coenzyme
Escherichia coli
0.049
-
D-malate
NAD+ as coenzyme
Escherichia coli
0.092
-
(+)-tartrate
thio-NAD+ as coenzyme
Escherichia coli
0.111
-
(+)-tartrate
NAD+ as coenzyme
Escherichia coli
0.83
-
(+)-tartrate
-
Escherichia coli
0.99
-
D-malate
-
Escherichia coli
1.63
-
D-malate
3-acetylpyridine-NAD+ as coenzyme
Escherichia coli
2.62
-
(+)-tartrate
3-acetylpyridine-NAD+ as coenzyme
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Reaction
Reaction
Commentary
Organism
meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+
enzyme catalyzes 3 different chemical reactions from a single active site
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-(+)-tartrate + NAD+
in presence of Mn2+ and K+ (+)-tartrate is subject to NAD+-dependent oxidation to form oxaloglycolate
349358
Escherichia coli
(3R)-oxaloglycolate + NADH
-
349358
Escherichia coli
?
malate + NAD+
oxidative decarboxylation in presence of Mn2+ and K+
349358
Escherichia coli
pyruvate + CO2 + NADH
-
349358
Escherichia coli
?
meso-tartrate + 3-acetylpyridine-NAD+
3-acetylpyridine-NAD+ is a very slow substrate for TDH
349358
Escherichia coli
D-glycerate + CO2 + ?
-
349358
Escherichia coli
?
meso-tartrate + NAD+
in presence of Mn2+ and K+ reaction requires only catalytic amounts of NAD+
349358
Escherichia coli
D-glycerate + CO2 + NADH
-
349358
Escherichia coli
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.417
-
(+)-tartrate
-
Escherichia coli
13.3
-
D-malate
-
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
3-acetylpyridine adenine dinucleotide
APAD
Escherichia coli
3-pyridinealdehyde adenine dinucleotide
PAAD
Escherichia coli
NAD+
-
Escherichia coli
thio-NAD+
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
Escherichia coli cells containing the plasmid pTDH1 which contains the gene encoding TDH under the control of the T7 polymerase promoter
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
3-acetylpyridine adenine dinucleotide
APAD
Escherichia coli
3-pyridinealdehyde adenine dinucleotide
PAAD
Escherichia coli
NAD+
-
Escherichia coli
thio-NAD+
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
oxalate
time-dependent inhibition
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.032
-
D-malate
thio-NAD+ as coenzyme
Escherichia coli
0.049
-
D-malate
NAD+ as coenzyme
Escherichia coli
0.092
-
(+)-tartrate
thio-NAD+ as coenzyme
Escherichia coli
0.111
-
(+)-tartrate
NAD+ as coenzyme
Escherichia coli
0.83
-
(+)-tartrate
-
Escherichia coli
0.99
-
D-malate
-
Escherichia coli
1.63
-
D-malate
3-acetylpyridine-NAD+ as coenzyme
Escherichia coli
2.62
-
(+)-tartrate
3-acetylpyridine-NAD+ as coenzyme
Escherichia coli
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-(+)-tartrate + NAD+
in presence of Mn2+ and K+ (+)-tartrate is subject to NAD+-dependent oxidation to form oxaloglycolate
349358
Escherichia coli
(3R)-oxaloglycolate + NADH
-
349358
Escherichia coli
?
malate + NAD+
oxidative decarboxylation in presence of Mn2+ and K+
349358
Escherichia coli
pyruvate + CO2 + NADH
-
349358
Escherichia coli
?
meso-tartrate + 3-acetylpyridine-NAD+
3-acetylpyridine-NAD+ is a very slow substrate for TDH
349358
Escherichia coli
D-glycerate + CO2 + ?
-
349358
Escherichia coli
?
meso-tartrate + NAD+
in presence of Mn2+ and K+ reaction requires only catalytic amounts of NAD+
349358
Escherichia coli
D-glycerate + CO2 + NADH
-
349358
Escherichia coli
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.417
-
(+)-tartrate
-
Escherichia coli
13.3
-
D-malate
-
Escherichia coli
Other publictions for EC 1.3.1.7
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)
349359
Serfozo
Substrate determinants of the ...
Escherichia coli, Pseudomonas putida
Biochemistry
34
7517-7524
1995
-
-
1
-
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-
13
-
-
-
-
-
2
-
-
1
-
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17
-
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1
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13
-
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-
1
-
-
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-
17
-
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-
-
-
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-
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-
-
-
-
-
-
349358
Beecher
Tartrate dehydrogenase-oxalate ...
Escherichia coli
Arch. Biochem. Biophys.
315
255-261
1994
-
-
1
-
-
-
1
8
-
-
-
-
-
1
-
-
1
1
-
-
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4
-
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2
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4
-
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-
1
4
-
-
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-
1
-
8
-
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-
-
-
-
-
1
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4
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2
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287509
Do Nascimento
The stereospecificity of seque ...
Pseudomonas putida, Pseudomonas putida ATCC 17642
Biochem. J.
149
553-557
1975
-
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-
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2
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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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-
349356
Kohn
-
L- and mesotartaric acid dehyd ...
Bos taurus, Pseudomonas putida, Pseudomonas sp., Pseudomonas sp. A, Rattus norvegicus
Methods Enzymol.
9
236-240
1966
1
-
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1
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4
2
1
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3
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9
-
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1
-
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1
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5
-
-
-
-
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2
-
-
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-
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-
1
-
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-
1
-
-
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4
2
1
-
3
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-
1
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1
-
5
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2
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