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Information on EC 1.1.1.93 - tartrate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.93
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.93 tartrate dehydrogenase
IUBMB Comments
meso-tartrate and (R,R)-tartrate act as substrates. Requires Mn2+ and a monovalent cation.
The enzyme appears in viruses and cellular organisms
- 1.1.1.93
- putida
- meso-tartrate
- d-malate
-
+-tartrate
-
hydride
-
nad-dependent
- isocitrate
-
agrobacterium
- oxalate
-
monovalent
- vitis
-
enolate
- isopropylmalate
-
dehydrogenase-catalyzed
- analysis
- sphaeroides
-
rhodopseudomonas
- decarboxylases
-
ion-dependent
- tartronate
-
grapevine
showSynonyms
tartrate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dehydrogenase, tartrate
-
-
-
-
mesotartrate dehydrogenase
-
-
-
-
TDH
TDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tartrate + NAD+ = oxaloglycolate + NADH + H+
primarily ordered mechanism
-
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
-
tartrate + NAD+ = oxaloglycolate + NADH + H+
kinetic mechanism, equilibrium-ordered addition of Mn2+ prior to D-malate or meso-tartrate, overview
-
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
-
tartrate + NAD+ = oxaloglycolate + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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CAS REGISTRY NUMBER
COMMENTARY
37250-29-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(+)-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(2R,3R)-3-bromomalate + NAD+
3-bromopyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3R)-3-chloromalate + NAD+
3-chloropyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3R)-3-fluoromalate + NAD+
3-fluoropyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3R)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3R)-3-methyltartrate + NAD+
? + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3S)-3-aminomalate + NAD+
3-aminopyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3S)-3-bromomalate + NAD+
3-bromopyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3S)-3-chloromalate + NAD+
3-chloropyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3S)-3-fluoromalate + NAD+
3-fluoropyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3S)-3-iodomalate + NAD+
3-iodopyruvate + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
(2R,3S)-3-methyltartrate + NAD+
? + NADH + CO2
-
Substrates: -
Products: -
Products: -
?
D-malate + thio-NAD+
pyruvate + CO2 + thio-NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-(+)-tartrate + NAD+
oxaloglycolate + NADH
-
Substrates: enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
Products: -
Products: -
?
D-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: -
Products: -
?
D-malate + NAD+
pyruvate + CO2 + NADH
-
Substrates: -
Products: D-malate is oxidized to oxaloacetate, which remains bound to the enzyme and undergoes decarboxylation to yield pyruvate
Products: D-malate is oxidized to oxaloacetate, which remains bound to the enzyme and undergoes decarboxylation to yield pyruvate
?
D-malate + NAD+
pyruvate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
pyruvate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
pyruvate + CO2 + NADH + H+
-
Substrates: stepwise oxidative decarboxylation, a oxalacetate intermediate is formed
Products: -
Products: -
?
D-malate + NAD+
pyruvate + CO2 + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
Products: dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
Products: dihydroxyfumarate is in tautomeric equilibrium with oxaloglycolate
?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: oxidation occurs at 2R position
Products: 3R-oxaloglycolate
Products: 3R-oxaloglycolate
?
L-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: oxidation occurs at 2R oposition
Products: meso-tartrate is oxidized to 3S-oxaloglycolate, followed by decarboxylation to hydroxypyruvate
Products: meso-tartrate is oxidized to 3S-oxaloglycolate, followed by decarboxylation to hydroxypyruvate
?
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
-
Substrates: random substrate binding
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-(+)-tartrate + NAD+
oxaloglycolate + NADH
-
Substrates: enzyme production is induced by growth on L-(+)-tartrate as the sole carbon source
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
additional information
-
the reaction requires a divalent metal ion for activity
Mn2+
-
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
oxalate
-
forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
thermodynamics, isothermal titration calorimetry study, kinetic mechanism, overview
-
0.079
D-malate
-
wild-type, pH 7.5, temperature not specified in the publication
0.093
D-malate
-
mutant R108Q, pH 7.5, temperature not specified in the publication
0.098
D-malate
-
mutant R98Q, pH 7.5, temperature not specified in the publication
0.18
D-malate
-
mutant R108L, pH 7.5, temperature not specified in the publication
0.025
NAD+
-
wild-type, pH 7.5, temperature not specified in the publication
0.096
NAD+
-
mutant R98Q, pH 7.5, temperature not specified in the publication
0.135
NAD+
-
mutant R108Q, pH 7.5, temperature not specified in the publication
0.24
NAD+
-
mutant R108L, pH 7.5, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
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
-
0.015
NAD+
-
mutant D225A, pH 7.5, temperature not specified in the publication
0.06
NAD+
-
mutant R108Q, pH 7.5, temperature not specified in the publication
0.087
NAD+
-
mutant R108L, pH 7.5, temperature not specified in the publication
0.088
NAD+
-
mutant D250A, pH 7.5, temperature not specified in the publication
0.175
NAD+
-
mutant R98Q, pH 7.5, temperature not specified in the publication
6.5
NAD+
-
wild-type, pH 7.5, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.48
D-malate
-
mutant R108L, pH 7.5, temperature not specified in the publication
1.8
D-malate
-
mutant R98Q, pH 7.5, temperature not specified in the publication
6.2
D-malate
-
mutant R108Q, pH 7.5, temperature not specified in the publication
82
D-malate
-
wild-type, pH 7.5, temperature not specified in the publication
0.36
NAD+
-
mutant R108L, pH 7.5, temperature not specified in the publication
1.8
NAD+
-
mutant R98Q, pH 7.5, temperature not specified in the publication
4.3
NAD+
-
mutant R108Q, pH 7.5, temperature not specified in the publication
260
NAD+
-
wild-type, pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4 - 9
-
bifunctional L-(+)-tartrate dehydrogenase/D-(+)-malate dehydrogenase (decarboxylating) EC 1.1.1.93/EC 1.1.1.83
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.8
-
pH 6: about 40% of activity maximum, pH 7.8: about 80% of activity maximum, dihydroxyfumarate + NADH
7 - 9
-
at pH 7 and pH 9: about 50% of activity maximum, mesotartrate + NAD+
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional L-tartrate dehydrogenase/D-malate dehydrogenase (decarboxylating), EC 1.1.1.93/EC 1.1.1.83
-
-
brenda
enzyme expressed in Escherichia coli carrying the plasmid pTDH1, which expresses the gene encoding TDH at high levels
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (1192 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36800
-
4 * 36800, sedimentation study after dialysis with guanidine-mercaptoethanol solution
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
tetramer
-
4 * 36800, sedimentation study after dialysis with guanidine-mercaptoethanol solution
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with the intermediate analog oxalate, Mg2+ and NADH, to 2.0 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
-
mutation in metal ion-binding ligand, 10fold decrease in metal ion-binding affinity and a two-orders-of-magnitude decrease in catalysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing and thawing of purified enzyme, 10-40% loss of activity
-
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
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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
-
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
-
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
brenda
Tipton, P.A.
Tartrate dehydrogenase, an enzyme with multiple catalytic activities
Protein Pept. Lett.
7
323-332
2000
Pseudomonas putida
-
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
-
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
EXTERNAL LINKS (specific for EC-Number 1.1.1.93)
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