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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
tartrate dehydrogenase, TDH,
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tartrate dehydrogenase
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meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+
meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+
enzyme catalyzes 3 different chemical reactions from a single active site
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meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+
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oxidative decarboxylation
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meso-tartrate:NAD+ oxidoreductase
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(2R,3R)-3-bromomalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3R)-3-chloromalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3R)-3-fluoromalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3R)-3-iodomalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3R)-3-methyltartrate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3R)-3-thiomalate + NAD+
?
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?
(2R,3S)-3-bromomalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3S)-3-chloromalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3S)-3-fluoromalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3S)-3-iodomalate + NAD+
? + CO2 + NADH
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oxidative decarboxylation
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?
(2R,3S)-3-methyltartrate + NAD+
? + NADH
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simple oxidation
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?
(2R,3S)-3-thiomalate + NAD+
?
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net non-oxidative decarboxylation
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?
D-malate + 3-acetylpyridine adenine dinucleotide
pyruvate + CO2 + reduced 3-acetylpyridine adenine dinucleotide
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r
D-malate + 3-pyridinealdehyde adenine dinucleotide
pyruvate + CO2 + reduced 3-pyridinealdehyde adenine dinucleotide
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r
D-malate + NAD+
pyruvate + CO2 + NADH
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r
D-malate + NAD+
pyruvate + CO2 + NADH + H+
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r
D-malate + thio-NAD+
pyruvate + CO2 + thio-NADH
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r
dihydroxyfumaric acid + NADH
meso-tartrate + NAD+
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r
L-(+)-tartrate + NAD+
(3R)-oxaloglycolate + NADH
malate + NAD+
pyruvate + CO2 + NADH + H+
meso-tartrate + 3-acetylpyridine-NAD+
D-glycerate + CO2 + ?
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3-acetylpyridine-NAD+ is a very slow substrate for TDH
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?
meso-tartrate + NAD+
D-glycerate + CO2 + NADH + H+
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
additional information
?
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3R-oxaloglycolate, (2R,3S)-3-aminomalate and (2R,3R)-3-aminomalate are no substrates
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?
L-(+)-tartrate + NAD+
(3R)-oxaloglycolate + NADH
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in presence of Mn2+ and K+ (+)-tartrate is subject to NAD+-dependent oxidation to form oxaloglycolate
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?
L-(+)-tartrate + NAD+
(3R)-oxaloglycolate + NADH
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in presence of Mn2+ and K+ (+)-tartrate is subject to NAD+-dependent oxidation to form oxaloglycolate
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?
L-(+)-tartrate + NAD+
(3R)-oxaloglycolate + NADH
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?
malate + NAD+
pyruvate + CO2 + NADH + H+
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?
malate + NAD+
pyruvate + CO2 + NADH + H+
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oxidative decarboxylation in presence of Mn2+ and K+
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?
meso-tartrate + NAD+
D-glycerate + CO2 + NADH + H+
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?
meso-tartrate + NAD+
D-glycerate + CO2 + NADH + H+
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in presence of Mn2+ and K+ reaction requires only catalytic amounts of NAD+
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?
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
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r
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
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r
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
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r
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
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?
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meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
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meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
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r
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH + H+
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r
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3-acetylpyridine adenine dinucleotide
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APAD
3-pyridinealdehyde adenine dinucleotide
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PAAD
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oxalate
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time-dependent inhibition
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0.092 - 2.62
(+)-tartrate
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
(2R,3R)-3-iodomalate
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0.06
(2R,3R)-3-methyltartrate
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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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0.027
(2R,3S)-3-iodomalate
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0.07
(2R,3S)-3-methyltartrate
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0.06 - 0.45
meso-tartrate
0.092
(+)-tartrate
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thio-NAD+ as coenzyme
0.111
(+)-tartrate
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NAD+ as coenzyme
2.62
(+)-tartrate
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3-acetylpyridine-NAD+ as coenzyme
0.032
D-malate
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thio-NAD+ as coenzyme
0.049
D-malate
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NAD+ as coenzyme
1.63
D-malate
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3-acetylpyridine-NAD+ as coenzyme
0.06
meso-tartrate
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0.06
NAD+
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6.5
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dihydroxyfumarate and NADH as substrate
8.5
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50% of optimal activity at pH 7 and 9
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cow
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brenda
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brenda
A.T.C.C.17642
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brenda
A
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brenda
A
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brenda
rat
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brenda
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brenda
A.T.C.C.17642
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brenda
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brenda
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brenda
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Escherichia coli cells containing the plasmid pTDH1 which contains the gene encoding TDH under the control of the T7 polymerase promoter
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gene encoding TDH cloned into the pET3a expression vector
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Do Nascimento, K.H.; Davies, D.D.
The stereospecificity of sequential nicotinamide-adenine dinucleotide-dependent oxidoreductases in relation to the evolution of metabolic sequences
Biochem. J.
149
553-557
1975
Pseudomonas putida, Pseudomonas putida ATCC 17642
brenda
Kohn, L.D.; Jakoby, W.B.
L- and mesotartaric acid dehydrogenase (crystalline)
Methods Enzymol.
9
236-240
1966
Bos taurus, Pseudomonas sp., Pseudomonas putida, Rattus norvegicus, Pseudomonas sp. A
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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
Escherichia coli
brenda
Serfozo, P.; Tipton, P.A.
Substrate determinants of the course of tartrate dehydrogenase-catalyzed reactions
Biochemistry
34
7517-7524
1995
Escherichia coli, Pseudomonas putida
brenda
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1.3.1.7 meso-tartrate dehydrogenase
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