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Literature summary extracted from

  • Tipton, P.A.; Beecher, B.S.
    Tartrate dehydrogenase, a new member of the family of metal-dependent decarboxylating R-hydroxyacid dehydrogenases (1994), Arch. Biochem. Biophys., 313, 15-21.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.93 expression in Escherichia coli Pseudomonas putida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.93 0.014
-
beta-isopropylmalate
-
Pseudomonas putida
1.1.1.93 0.06
-
D-malate
-
Pseudomonas putida
1.1.1.93 1
-
L-Tartrate
-
Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.93 40636
-
x * 40636, calculation from nucleotide sequence Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.93 Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.93 isopropylmalate + NAD+
-
Pseudomonas putida ?
-
?
1.1.1.93 L-tartrate + NAD+
-
Pseudomonas putida oxaloglycolate + NADH + H+
-
?

Subunits

EC Number Subunits Comment Organism
1.1.1.93 ? x * 40636, calculation from nucleotide sequence Pseudomonas putida

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.93 0.167
-
isopropylmalate
-
Pseudomonas putida
1.1.1.93 0.417
-
L-Tartrate
-
Pseudomonas putida
1.1.1.93 13.3
-
D-malate
-
Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.93 NAD+ cofactor Pseudomonas putida