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Literature summary for 1.1.1.38 extracted from

  • Landsperger, W.J.; Harris, B.G.
    NAD+-malic enzyme. Regulatory properties of the enzyme from Ascaris suum (1976), J. Biol. Chem., 251, 3599-3602.
    View publication on PubMed
Search for more literature for 1.1.1.38

Activating Compound

Activating Compound Comment Organism Structure
fumarate 0.7 mM, 2.1fold activation Ascaris suum

Inhibitors

Inhibitors Comment Organism Structure
2-methylbutanoate 5.22 mM, competitive inhibitor, 60% inhibition at pH 7.5, 54% inhibition at pH 7.0 Ascaris suum
2-methylpentanoate 5.22 mM, competitive inhibitor, 45% inhibition at pH 7.5, 40% inhibition at pH 7.0 Ascaris suum
oxaloacetate 1 mM, 80% inhibition at pH 7.5, 50% inhibition at pH 7.0 Ascaris suum
tiglic acid 5.22 mM, competitive inhibitor, 58% inhibition at pH 7.5, 52% inhibition at pH 7.0 Ascaris suum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
 NAD+ at pH 6.5, 7.0 and 7.5 Ascaris suum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Ascaris suum 5739
-

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
-
 parasitic roundwurm
-

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