Information on EC 1.3.1.7 - meso-tartrate dehydrogenase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.1.7
-
RECOMMENDED NAME
GeneOntology No.
meso-tartrate dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
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redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
meso-tartrate:NAD+ oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37251-06-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cow
-
-
Manually annotated by BRENDA team
A.T.C.C.17642
-
-
Manually annotated by BRENDA team
A
-
-
Manually annotated by BRENDA team
A
-
-
Manually annotated by BRENDA team
rat
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-3-bromomalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3R)-3-chloromalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3R)-3-fluoromalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3R)-3-iodomalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3R)-3-methyltartrate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3R)-3-thiomalate + NAD+
?
show the reaction diagram
-
-
-
-
?
(2R,3S)-3-bromomalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3S)-3-chloromalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3S)-3-fluoromalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3S)-3-iodomalate + NAD+
? + CO2 + NADH
show the reaction diagram
-
oxidative decarboxylation
-
-
?
(2R,3S)-3-methyltartrate + NAD+
? + NADH
show the reaction diagram
-
simple oxidation
-
-
?
(2R,3S)-3-thiomalate + NAD+
?
show the reaction diagram
-
net non-oxidative decarboxylation
-
-
?
dihydroxyfumaric acid + NADH
meso-tartrate + NAD+
show the reaction diagram
-
-
-
-
r
L-(+)-tartrate + NAD+
(3R)-oxaloglycolate + NADH
show the reaction diagram
malate + NAD+
pyruvate + CO2 + NADH
show the reaction diagram
meso-tartrate + 3-acetylpyridine-NAD+
D-glycerate + CO2 + ?
show the reaction diagram
-
3-acetylpyridine-NAD+ is a very slow substrate for TDH
-
?
meso-tartrate + NAD+
D-glycerate + CO2 + NADH
show the reaction diagram
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH
show the reaction diagram
meso-tartrate + NAD+
oxaloglycolate + NADH + H+
show the reaction diagram
additional information
?
-
-
3R-oxaloglycolate, (2R,3S)-3-aminomalate and (2R,3R)-3-aminomalate are no substrates
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-
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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
meso-tartrate + NAD+
dihydroxyfumaric acid + NADH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-acetylpyridine adenine dinucleotide
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APAD
3-pyridinealdehyde adenine dinucleotide
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PAAD
thio-NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
oxalate
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time-dependent inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
mercaptan
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.092 - 2.62
(+)-tartrate
0.22
(2R,3R)-3-bromomalate
-
-
0.27
(2R,3R)-3-chloromalate
-
-
0.67
(2R,3R)-3-fluoromalate
-
-
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
-
-
0.012
(2R,3S)-3-chloromalate
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-
0.019
(2R,3S)-3-fluoromalate
-
-
0.027
(2R,3S)-3-iodomalate
-
-
0.07
(2R,3S)-3-methyltartrate
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-
0.032 - 1.63
D-malate
7.2
L(+)-Tartrate
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-
0.06 - 0.45
meso-tartrate
0.06 - 0.15
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.417
(+)-tartrate
Escherichia coli
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13.3
D-malate
Escherichia coli
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
dihydroxyfumarate and NADH as substrate
8.5
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50% of optimal activity at pH 7 and 9
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
rectangular prisms
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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