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Literature summary 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)

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.93 oxalate forms a stable complex with Mn-tartrate dehydrogenase-NADH complexes Pseudomonas putida
1.3.1.7 oxalate time-dependent inhibition Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.7 0.032
-
 D-malate thio-NAD+ as coenzyme Escherichia coli
1.3.1.7 0.049
-
 D-malate NAD+ as coenzyme Escherichia coli
1.3.1.7 0.092
-
 (+)-tartrate thio-NAD+ as coenzyme Escherichia coli
1.3.1.7 0.111
-
 (+)-tartrate NAD+ as coenzyme Escherichia coli
1.3.1.7 0.83
-
 (+)-tartrate
-
 Escherichia coli
1.3.1.7 0.99
-
 D-malate
-
 Escherichia coli
1.3.1.7 1.63
-
 D-malate 3-acetylpyridine-NAD+ as coenzyme Escherichia coli
1.3.1.7 2.62
-
 (+)-tartrate 3-acetylpyridine-NAD+ as coenzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.93 Pseudomonas putida
-
 expression by Escherichia coli
-
1.3.1.7 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.7
-
 Escherichia coli

Reaction

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.3.1.7 tartrate dehydrogenase
-
 Escherichia coli
1.3.1.7 TDH
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.7 0.417
-
 (+)-tartrate
-
 Escherichia coli
1.3.1.7 13.3
-
 D-malate
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.93 NAD+ cofactor Pseudomonas putida
1.3.1.7 3-acetylpyridine adenine dinucleotide APAD Escherichia coli
1.3.1.7 3-pyridinealdehyde adenine dinucleotide PAAD Escherichia coli
1.3.1.7 NAD+
-
 Escherichia coli
1.3.1.7 thio-NAD+
-
 Escherichia coli