Information on EC 1.1.1.93 - tartrate dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.93
-
RECOMMENDED NAME
GeneOntology No.
tartrate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
tartrate + NAD+ = oxaloglycolate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
tartrate:NAD+ oxidoreductase
meso-tartrate and (R,R)-tartrate act as substrates. Requires Mn2+ and a monovalent cation.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-29-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+)-tartrate + NAD+
oxaloglycolate + NADH + H+
show the reaction diagram
-
-
-
-
?
(2R,3R)-3-bromomalate + NAD+
3-bromopyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3R)-3-chloromalate + NAD+
3-chloropyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3R)-3-fluoromalate + NAD+
3-fluoropyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3R)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
show the reaction diagram
(2R,3R)-3-methyltartrate + NAD+
? + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3S)-3-aminomalate + NAD+
3-aminopyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3S)-3-bromomalate + NAD+
3-bromopyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3S)-3-chloromalate + NAD+
3-chloropyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3S)-3-fluoromalate + NAD+
3-fluoropyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3S)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
show the reaction diagram
-
-
-
?
(2R,3S)-3-methyltartrate + NAD+
? + NADH + CO2
show the reaction diagram
-
-
-
?
D-malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
D-malate + NAD+
pyruvate + CO2 + NADH + H+
show the reaction diagram
D-malate + thio-NAD+
pyruvate + CO2 + thio-NADH + H+
show the reaction diagram
-
-
-
-
?
isopropylmalate + NAD+
?
show the reaction diagram
-
-
-
-
?
L-(+)-tartrate + NAD+
oxaloglycolate + NADH
show the reaction diagram
-
enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
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-
-
L-tartrate + NAD+
oxaloglycolate + NADH + H+
show the reaction diagram
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
show the reaction diagram
oxaloglycolate + NADH
tartrate + NAD+
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-(+)-tartrate + NAD+
oxaloglycolate + NADH
show the reaction diagram
-
enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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cofactor
thio-NAD+
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-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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1 mM, 30% of the activation with 0.4 mM MnCl2
NaCl
-
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+
-
0.1 mM, 14% of the activation with 0.4 mM MnCl2
additional information
-
the reaction requires a divalent metal ion for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-malate
-
competitive versus L-tartrate and meso-tartate
Dihydroxyfumarate
-
-
L-Tartrate
-
competitive versus meso-tartrate and D-malate
meso-tartrate
NADH
-
competitive versus NAD+
oxalate
-
forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes
oxaloacetate
-
competitive
Tartronate
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inhibition of oxidative decarboxylation of D-malate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
-
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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-
0.05 - 0.18
D-malate
11
Dihydroxyfumarate
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in presence of 0.19 mM NADH
0.014
isopropylmalate
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-
1 - 55
L-Tartrate
0.06 - 0.83
meso-tartrate
0.025 - 0.28
NAD+
1.4
NADH
-
in presence of 1.5 mM dihydroxyfumarate
additional information
additional information
-
thermodynamics, isothermal titration calorimetry study, kinetic mechanism, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.3 - 19.7
D-malate
0.167 - 0.2
isopropylmalate
0.417 - 0.483
L-Tartrate
0.617
meso-tartrate
Pseudomonas putida
-
-
0.015 - 6.5
NAD+
additional information
additional information
Pseudomonas putida
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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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48 - 82
D-malate
1139
0.36 - 260
NAD+
7
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
dihydroxyfumarate + NADH
8
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assay at
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+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 - 9
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at pH 7 and pH 9: about 50% of activity maximum, mesotartrate + NAD+
7 - 10.6
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at pH 7.0 and pH 10.6: 50% of activity maximum
additional information
-
discussion of the pH-rate profile of the reaction with D-malate or (+)-tartrate, the pH dependence of the pyruvate/malate ratio is studied
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
77000
-
gel filtration
145000
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diffusion and sedimentation data
158000
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gel filtration
162000
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ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 40636, calculation from nucleotide sequence
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with the intermediate analog oxalate, Mg2+ and NADH, to 2.0 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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pH 7.0, 30 h: 50% loss of activity. pH 8.5, stable for 4 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, months, partially purified enzyme
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4°C, in 10% glycerol, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D225A
-
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
-
1.3% of wild-type catalytic rate
R108Q
-
8.7% of wild-type catalytic rate
R98L
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mutant is not expressed in stable form
R98Q
-
2.6% of wild-type catalytic rate
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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