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EC Tree
IUBMB Comments meso-tartrate and (R,R)-tartrate act as substrates. Requires Mn2+ and a monovalent cation.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
tartrate dehydrogenase,
more
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dehydrogenase, tartrate
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mesotartrate dehydrogenase
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TDH
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tartrate + NAD+ = oxaloglycolate + NADH + H+
tartrate + NAD+ = oxaloglycolate + NADH + H+
primarily ordered mechanism
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tartrate + NAD+ = oxaloglycolate + NADH + H+
A-side dehydrogenase, i.e. the hydride is transferred from the substrate to the pro-R position of C4 of NADH
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tartrate + NAD+ = oxaloglycolate + NADH + H+
kinetic mechanism, equilibrium-ordered addition of Mn2+ prior to D-malate or meso-tartrate, overview
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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
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tartrate + NAD+ = oxaloglycolate + NADH + H+
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tartrate:NAD+ oxidoreductase
meso-tartrate and (R,R)-tartrate act as substrates. Requires Mn2+ and a monovalent cation.
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(+)-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
(2R,3R)-3-aminomalate + NAD+
?
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r
(2R,3R)-3-bromomalate + NAD+
3-bromopyruvate + NADH + CO2
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?
(2R,3R)-3-chloromalate + NAD+
3-chloropyruvate + NADH + CO2
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?
(2R,3R)-3-fluoromalate + NAD+
3-fluoropyruvate + NADH + CO2
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?
(2R,3R)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
(2R,3R)-3-methyltartrate + NAD+
? + NADH + CO2
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-
?
(2R,3S)-3-aminomalate + NAD+
3-aminopyruvate + NADH + CO2
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?
(2R,3S)-3-bromomalate + NAD+
3-bromopyruvate + NADH + CO2
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?
(2R,3S)-3-chloromalate + NAD+
3-chloropyruvate + NADH + CO2
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?
(2R,3S)-3-fluoromalate + NAD+
3-fluoropyruvate + NADH + CO2
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?
(2R,3S)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
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?
(2R,3S)-3-methyltartrate + NAD+
? + NADH + CO2
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?
D-malate + NAD+
pyruvate + CO2 + NADH
D-malate + NAD+
pyruvate + CO2 + NADH + H+
D-malate + thio-NAD+
pyruvate + CO2 + thio-NADH + H+
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?
dihydroxyfumarate + NAD+
?
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r
isopropylmalate + NAD+
?
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?
L-(+)-tartrate + NAD+
oxaloglycolate + NADH
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enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
oxaloglycolate + NADH
tartrate + NAD+
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r
(2R,3R)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
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?
(2R,3R)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
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?
D-malate + NAD+
pyruvate + CO2 + NADH
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?
D-malate + NAD+
pyruvate + CO2 + NADH
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?
D-malate + NAD+
pyruvate + CO2 + NADH
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D-malate is oxidized to oxaloacetate, which remains bound to the enzyme and undergoes decarboxylation to yield pyruvate
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D-malate + NAD+
pyruvate + CO2 + NADH + H+
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r
D-malate + NAD+
pyruvate + CO2 + NADH + H+
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r
D-malate + NAD+
pyruvate + CO2 + NADH + H+
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stepwise oxidative decarboxylation, a oxalacetate intermediate is formed
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?
D-malate + NAD+
pyruvate + CO2 + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
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L-tartrate + NAD+
oxaloglycolate + NADH + H+
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dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
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L-tartrate + NAD+
oxaloglycolate + NADH + H+
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L-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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r
L-tartrate + NAD+
oxaloglycolate + NADH + H+
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oxidation occurs at 2R position
3R-oxaloglycolate
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meso-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
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r
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
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oxidation occurs at 2R oposition
meso-tartrate is oxidized to 3S-oxaloglycolate, followed by decarboxylation to hydroxypyruvate
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meso-tartrate + NAD+
oxaloglycolate + NADH + H+
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random substrate binding
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?
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L-(+)-tartrate + NAD+
oxaloglycolate + NADH
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enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
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NAD+
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NAD+
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binding stoichiometry, random binding
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Co2+
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1 mM, 30% of the activation with 0.4 mM MnCl2
NaCl
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50 mM KCl, 19% of the activation with 50 mM NH4Cl
Rb+
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monovalent cation required, maximal activity with K+ and Rb+
Zn2+
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0.1 mM, 14% of the activation with 0.4 mM MnCl2
additional information
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the reaction requires a divalent metal ion for activity
K+
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50 mM KCl, 63% of the activation with 50 mM NH4Cl
K+
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50 mM K2SO4, 56% of the activation with 50 mM KCl
K+
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monovalent cation required, maximal activity with K+ and Rb+
K+
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required for binding of meso-tartrate
Mg2+
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5 mM, 59% of the activation with 0.4 mM MnCl2
Mg2+
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optimal concentration: 50 mM
Mg2+
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supports catalytic activity
Mn2+
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Km: 0.016 mM, reaction with L-malate or D-malate
Mn2+
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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
Mn2+
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supports catalytic activity
Mn2+
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required for binding of meso-tartrate
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D-malate
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competitive versus L-tartrate and meso-tartate
L-Tartrate
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competitive versus meso-tartrate and D-malate
NADH
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competitive versus NAD+
oxalate
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forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes
oxaloacetate
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competitive
Tartronate
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inhibition of oxidative decarboxylation of D-malate
meso-tartrate
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competitive
meso-tartrate
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competitive versus L-tartrate and D-malate
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NH4+
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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
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0.58
(2R,3R)-3-aminomalate
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0.22
(2R,3R)-3-bromomalate
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0.27
(2R,3R)-3-chloromalate
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0.67
(2R,3R)-3-fluoromalate
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0.024 - 0.027
(2R,3R)-3-iodomalate
0.06 - 0.07
(2R,3R)-3-methyltartrate
0.026
(2R,3S)-3-aminomalate
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0.011
(2R,3S)-3-bromomalate
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0.012
(2R,3S)-3-chloromalate
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0.019
(2R,3S)-3-fluoromalate
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0.014
beta-isopropylmalate
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11
Dihydroxyfumarate
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in presence of 0.19 mM NADH
0.014
isopropylmalate
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0.06 - 0.83
meso-tartrate
1.4
NADH
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in presence of 1.5 mM dihydroxyfumarate
additional information
additional information
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thermodynamics, isothermal titration calorimetry study, kinetic mechanism, overview
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0.024
(2R,3R)-3-iodomalate
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0.027
(2R,3R)-3-iodomalate
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0.06
(2R,3R)-3-methyltartrate
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0.07
(2R,3R)-3-methyltartrate
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0.05
D-malate
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0.079
D-malate
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wild-type, pH 7.5, temperature not specified in the publication
0.093
D-malate
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mutant R108Q, pH 7.5, temperature not specified in the publication
0.098
D-malate
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mutant R98Q, pH 7.5, temperature not specified in the publication
0.18
D-malate
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mutant R108L, pH 7.5, temperature not specified in the publication
1
L-Tartrate
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0.06
meso-tartrate
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0.025
NAD+
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wild-type, pH 7.5, temperature not specified in the publication
0.096
NAD+
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mutant R98Q, pH 7.5, temperature not specified in the publication
0.13
NAD+
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reaction with D-malate
0.135
NAD+
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mutant R108Q, pH 7.5, temperature not specified in the publication
0.24
NAD+
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mutant R108L, pH 7.5, temperature not specified in the publication
0.28
NAD+
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reaction with (+ L-(+)-tartrate)
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0.167 - 0.2
isopropylmalate
additional information
additional information
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D-malate oxidation is largely limited by the rate of decarboxylation of the intermediate oxaloacetate which occurs at 660 per min. Hydride transfer from D-malate to NAD+ occurs with a rate constant of 1800 per min
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13.3
D-malate
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0.167
isopropylmalate
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0.417
L-Tartrate
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0.015
NAD+
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mutant D225A, pH 7.5, temperature not specified in the publication
0.06
NAD+
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mutant R108Q, pH 7.5, temperature not specified in the publication
0.087
NAD+
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mutant R108L, pH 7.5, temperature not specified in the publication
0.088
NAD+
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mutant D250A, pH 7.5, temperature not specified in the publication
0.175
NAD+
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mutant R98Q, pH 7.5, temperature not specified in the publication
6.5
NAD+
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wild-type, pH 7.5, temperature not specified in the publication
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0.48
D-malate
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mutant R108L, pH 7.5, temperature not specified in the publication
1.8
D-malate
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mutant R98Q, pH 7.5, temperature not specified in the publication
6.2
D-malate
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mutant R108Q, pH 7.5, temperature not specified in the publication
82
D-malate
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wild-type, pH 7.5, temperature not specified in the publication
0.36
NAD+
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mutant R108L, pH 7.5, temperature not specified in the publication
1.8
NAD+
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mutant R98Q, pH 7.5, temperature not specified in the publication
4.3
NAD+
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mutant R108Q, pH 7.5, temperature not specified in the publication
260
NAD+
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wild-type, pH 7.5, temperature not specified in the publication
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7
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dihydroxyfumarate + NADH
8.4 - 9
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bifunctional L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83
8.5
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meso-tartrate + NAD+
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6 - 7.8
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pH 6: about 40% of activity maximum, pH 7.8: about 80% of activity maximum, dihydroxyfumarate + NADH
7 - 10.6
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at pH 7.0 and pH 10.6: 50% of activity maximum
7 - 9
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at pH 7 and pH 9: about 50% of activity maximum, mesotartrate + NAD+
additional information
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discussion of the pH-rate profile of the reaction with D-malate or (+)-tartrate, the pH dependence of the pyruvate/malate ratio is studied
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brenda
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brenda
bifunctional L-tartrate dehydrogenase/D-malate dehydrogenase (decarboxylating), EC 1.1.1.93/EC 1.1.1.83
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brenda
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brenda
ATCC 17642
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brenda
enzyme expressed in Escherichia coli carrying the plasmid pTDH1, which expresses the gene encoding TDH at high levels
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brenda
expression by Escherichia coli
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brenda
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brenda
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145000
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diffusion and sedimentation data
162000
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ultracentrifugation
36800
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4 * 36800, sedimentation study after dialysis with guanidine-mercaptoethanol solution
38000
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2 * 38000, SDS-PAGE
38500
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4 * 38500, SDS-PAGE
40636
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x * 40636, calculation from nucleotide sequence
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?
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x * 40636, calculation from nucleotide sequence
dimer
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dimer
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2 * 38000, SDS-PAGE
tetramer
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4 * 38500, SDS-PAGE
tetramer
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4 * 38500, SDS-PAGE
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tetramer
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4 * 36800, sedimentation study after dialysis with guanidine-mercaptoethanol solution
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in complex with the intermediate analog oxalate, Mg2+ and NADH, to 2.0 A resolution
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D225A
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mutation in metal ion-binding ligand, 20fold decrease in metal ion-binding affinity and a two-orders-of-magnitude decrease in catalysis
D250A
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mutation in metal ion-binding ligand, 10fold decrease in metal ion-binding affinity and a two-orders-of-magnitude decrease in catalysis
R108L
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1.3% of wild-type catalytic rate
R108Q
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8.7% of wild-type catalytic rate
R98L
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mutant is not expressed in stable form
R98Q
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2.6% of wild-type catalytic rate
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30
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pH 7.0, 30 h: 50% loss of activity. pH 8.5, stable for 4 h
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repeated freezing and thawing of purified enzyme, 10-40% loss of activity
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the enzyme reactor is stored at 5°C in 0.1 M phosphate buffer, pH 8.0, 10 mM dithiothreitol, when not in use, 40% loss of activity after 1 week, then activity maintains a constant value for 1 month
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-20°C, months, partially purified enzyme
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4°C, in 10% glycerol, stable for several months
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bifunctional L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating), EC 1.1.1.93/EC 1.1.1.83
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methods that minimize the enzyme losses while achieving the target of removing the nucleic acids and undesirable enzymes, methods of precipitation of nucleic acids from the homogenates
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expression in Escherichia coli
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analysis
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determination of L-(+)-tartrate in wines and juices
analysis
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quantification of L-tartrate in wine by a stopped-flow injection system with an immobilized enzyme reactor and fluorescence detection, the enzyme is immobilized on aminopropyl-controlled pore glass beads with glutaraldehyde
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Ebbighausen, H.; Giffhorn, F.
A novel mechanism involved in the metabolism of the tartaric acid stereoisomers in Rhodopseudomonas sphaeroides: enzymatic conversion of meso-tartaric acid to D(-)-glyceric acid and CO2
Arch. Microbiol.
138
338-344
1984
Cereibacter sphaeroides
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brenda
Beecher, B.S.; Koder, R.L.; Tipton, P.A.
Tartrate dehydrogenase-oxalate complexes: formation of a stable analog of a reaction intermediate complex
Arch. Biochem. Biophys.
315
255-261
1994
Pseudomonas putida
brenda
Serfozo, P.; Tipton, P.A.
Substrate determinants of the course of tartrate dehydrogenase-catalyzed reactions
Biochemistry
34
7517-7524
1995
Pseudomonas putida
brenda
Giffhorn, F.; Kuhn, A.
Purification and characterization of a bifunctional L-(+)-tartrate dehydrogenase-D-(+)-malate dehydrogenase (decarboxylating) from Rhodopseudomonas sphaeroides Y
J. Bacteriol.
155
281-290
1983
Cereibacter sphaeroides
brenda
Kohn, L.D.; Packman, P.M.; Allen, R.H.; Jakoby, W.B.
Tartaric acid metabolism. V. Crystalline tartrate dehydrogenase
J. Biol. Chem.
243
2479-2485
1968
Pseudomonas putida
brenda
Gifforn, F.; Beutler, H.O.
L-(+)-Tartrate
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
7
78-85
1985
Cereibacter sphaeroides
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brenda
Tipton, P.A.
Tartrate dehydrogenase, an enzyme with multiple catalytic activities
Protein Pept. Lett.
7
323-332
2000
Pseudomonas putida
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brenda
Harve, R.; Bajpai, R.K.
Production and purification of tartrate dehydrogenase: role of aqueous two-phase extraction
Appl. Biochem. Biotechnol.
70-72
677-686
1998
Pseudomonas putida
brenda
Tipton, P.A.
Transient-state kinetic analysis of the oxidative decarboxylation of D-malate catalyzed by tartrate dehydrogenase
Biochemistry
35
3108-3114
1996
Pseudomonas putida
brenda
Tipton, P.A.; Beecher, B.S.
Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases
Arch. Biochem. Biophys.
313
15-21
1994
Pseudomonas putida
brenda
Tipton, P.A.; Peisach, J.
Characterization of the multiple catalytic activities of tartrate dehdrogenase
Biochemistry
29
1749-1756
1990
Pseudomonas putida
brenda
Tsukatani, T.; Matsumoto, K.
Quantification of L-tartrate in wine by stopped-flow injection analysis using immobilized D-malate dehydrogenase and fluorescence detection
Anal. Sci.
16
265-268
2000
Escherichia coli
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brenda
Karsten, W.E.; Tipton, P.A.; Cook, P.F.
Tartrate dehydrogenase catalyzes the stepwise oxidative decarboxylation of D-malate with both NAD and thio-NAD
Biochemistry
41
12193-12199
2002
Escherichia coli
brenda
Karsten, W.E.; Cook, P.F.
An isothermal titration calorimetry study of the binding of substrates and ligands to the tartrate dehydrogenase from Pseudomonas putida reveals half-of-the-sites reactivity
Biochemistry
45
9000-9006
2006
Pseudomonas putida
brenda
Malik, R.; Viola, R.E.
Structural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactions
Acta Crystallogr. Sect. D
66
673-684
2010
Pseudomonas putida
brenda
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