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Literature summary for 1.1.1.38 extracted from

  • Park, S-H.; Kiick, D.M.; Harris, B.G.; Cook, P.F.
    Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum (1984), Biochemistry, 23, 5446-5453.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cl- competitive vs. malate and NAD+ Ascaris suum
Tartronate competitive inhibition vs. malate, noncompetitve vs. NAD+ Ascaris suum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.004
-
NAD+ pH 9.0 Ascaris suum
0.011
-
NAD+ pH 7.3 Ascaris suum
1.18
-
L-malate pH 7.3 Ascaris suum
5.2
-
L-malate pH 9.0 Ascaris suum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Ascaris suum
-
CO2 + pyruvate + NADH
-
?
Oxaloacetate Ascaris suum
-
CO2 + pyruvate
-
ir

Organism

Organism UniProt Comment Textmining
Ascaris suum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
Ascaris suum CO2 + pyruvate + NADH
-
?
(S)-malate + NAD+
-
Ascaris suum CO2 + pyruvate + NADH
-
r
Oxaloacetate
-
Ascaris suum CO2 + pyruvate
-
ir

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Ascaris suum