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Literature summary for 1.3.1.7 extracted from

  • Beecher, B.S.; Koder, R.L.; Tipton, P.A.
    Tartrate dehydrogenase-oxalate complexes: formation of a stable analog of a reaction intermediate complex (1994), Arch. Biochem. Biophys., 315, 255-261.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli cells containing the plasmid pTDH1 which contains the gene encoding TDH under the control of the T7 polymerase promoter Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
oxalate time-dependent inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.032
-
D-malate thio-NAD+ as coenzyme Escherichia coli
0.049
-
D-malate NAD+ as coenzyme Escherichia coli
0.092
-
(+)-tartrate thio-NAD+ as coenzyme Escherichia coli
0.111
-
(+)-tartrate NAD+ as coenzyme Escherichia coli
0.83
-
(+)-tartrate
-
Escherichia coli
0.99
-
D-malate
-
Escherichia coli
1.63
-
D-malate 3-acetylpyridine-NAD+ as coenzyme Escherichia coli
2.62
-
(+)-tartrate 3-acetylpyridine-NAD+ as coenzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
meso-tartrate + NAD+ = dihydroxyfumarate + NADH + H+ enzyme catalyzes 3 different chemical reactions from a single active site Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-malate + 3-acetylpyridine adenine dinucleotide
-
Escherichia coli pyruvate + CO2 + reduced 3-acetylpyridine adenine dinucleotide
-
r
D-malate + 3-pyridinealdehyde adenine dinucleotide
-
Escherichia coli pyruvate + CO2 + reduced 3-pyridinealdehyde adenine dinucleotide
-
r
D-malate + NAD+
-
Escherichia coli pyruvate + CO2 + NADH
-
r
D-malate + NAD+
-
Escherichia coli pyruvate + CO2 + NADH + H+
-
r
D-malate + thio-NAD+
-
Escherichia coli pyruvate + CO2 + thio-NADH
-
r
L-(+)-tartrate + NAD+ in presence of Mn2+ and K+ (+)-tartrate is subject to NAD+-dependent oxidation to form oxaloglycolate Escherichia coli (3R)-oxaloglycolate + NADH
-
?
malate + NAD+ oxidative decarboxylation in presence of Mn2+ and K+ Escherichia coli pyruvate + CO2 + NADH + H+
-
?
meso-tartrate + 3-acetylpyridine-NAD+ 3-acetylpyridine-NAD+ is a very slow substrate for TDH Escherichia coli D-glycerate + CO2 + ?
-
?
meso-tartrate + NAD+ in presence of Mn2+ and K+ reaction requires only catalytic amounts of NAD+ Escherichia coli D-glycerate + CO2 + NADH + H+
-
?

Synonyms

Synonyms Comment Organism
tartrate dehydrogenase
-
Escherichia coli
TDH
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.417
-
(+)-tartrate
-
Escherichia coli
13.3
-
D-malate
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
3-acetylpyridine adenine dinucleotide APAD Escherichia coli
3-pyridinealdehyde adenine dinucleotide PAAD Escherichia coli
NAD+
-
Escherichia coli
thio-NAD+
-
Escherichia coli