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Literature summary for 1.1.1.39 extracted from

  • Hrdy, I.; Mertens, E.
    Purification and partial characterization of malate dehydrogenase (decarboxylating) from Tritrichomonas foetus hydrogenosomes (1993), Parasitology, 107, 379-385.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
NAD+
-
Tritrichomonas suis
0.1
-
(S)-malate with NAD+ as cofactor Tritrichomonas suis
0.207
-
NADP+
-
Tritrichomonas suis
0.458
-
(S)-malate with NADP+ as cofactor Tritrichomonas suis

Localization

Localization Comment Organism GeneOntology No. Textmining
hydrogenosome
-
Tritrichomonas suis 42566
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activation by Mn2+, at 1 mM, is 10% and 20% higher than activation with 1 mM Mg2+ in the presence of NAD+ and NADP+ Tritrichomonas suis
Mg2+ completely dependent on the presence of Mg2+ or Mn2+ Tritrichomonas suis
Mn2+ completely dependent on the presence of Mg2+ or Mn2+ Tritrichomonas suis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
308000
-
gel filtration Tritrichomonas suis

Organism

Organism UniProt Comment Textmining
Tritrichomonas suis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Tritrichomonas suis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
20.5
-
-
Tritrichomonas suis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NADP+
-
Tritrichomonas suis pyruvate + CO2 + NADPH
-
?
malate + NAD+
-
Tritrichomonas suis pyruvate + CO2 + NADH + H+
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+ cofactor Tritrichomonas suis
NADP+ activity is maximal 65% of the activity with NAD+ Tritrichomonas suis