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Literature summary for 1.1.1.93 extracted from

  • Karsten, W.E.; Cook, P.F.
    An isothermal titration calorimetry study of the binding of substrates and ligands to the tartrate dehydrogenase from Pseudomonas putida reveals half-of-the-sites reactivity (2006), Biochemistry, 45, 9000-9006.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information thermodynamics, isothermal titration calorimetry study, kinetic mechanism, overview Pseudomonas putida

Metals/Ions

Metals/Ions Comment Organism Structure
K+ required for binding of meso-tartrate Pseudomonas putida
Mn2+ required for binding of meso-tartrate Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Reaction

Reaction Comment Organism Reaction ID
tartrate + NAD+ = oxaloglycolate + NADH + H+ kinetic mechanism, equilibrium-ordered addition of Mn2+ prior to D-malate or meso-tartrate, overview Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-malate + NAD+
-
Pseudomonas putida pyruvate + CO2 + NADH + H+
-
?
meso-tartrate + NAD+ random substrate binding Pseudomonas putida oxaloglycolate + NADH + H+
-
?

Subunits

Subunits Comment Organism
dimer
-
Pseudomonas putida

Synonyms

Synonyms Comment Organism
TDH
-
Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Pseudomonas putida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
NAD+ binding stoichiometry, random binding Pseudomonas putida