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Literature summary for 1.1.1.93 extracted from

  • Tipton, P.A.
    Transient-state kinetic analysis of the oxidative decarboxylation of D-malate catalyzed by tartrate dehydrogenase (1996), Biochemistry, 35, 3108-3114.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Tartronate inhibition of oxidative decarboxylation of D-malate Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
(2R,3R)-3-iodomalate
-
Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
enzyme expressed in Escherichia coli carrying the plasmid pTDH1, which expresses the gene encoding TDH at high levels
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R,3R)-3-iodomalate + NAD+
-
Pseudomonas putida 3-iodopyruvate + NADH + CO2
-
?
D-malate + NAD+
-
Pseudomonas putida pyruvate + CO2 + NADH
-
?
L-tartrate + NAD+
-
Pseudomonas putida oxaloglycolate + NADH + H+
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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 Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
NAD+ cofactor Pseudomonas putida