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Literature summary extracted from

  • Karsten, W.E.; Pais, J.E.; Rao, G.S.; Harris, B.G.; Cook, P.F.
    Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites (2003), Biochemistry, 42, 9712-9721.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.39 fumarate activates in both reaction directions synergistically with L-malate both binding at separate allosteric sites different from the active site, R105 and K143 are involved Ascaris suum
1.1.1.39 L-malate activates in both reaction directions synergistically with fumarate both binding at separate allosteric sites different from the active site, R105 and K143 are involved Ascaris suum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.39 expression of mutant enzymes in Escherichia coli strain M15 Ascaris suum

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.39 K143A site-directed mutagenesis, malate binding residue, mutant shows highly increased kcat for malate and fumarate compared to the wild-type enzyme Ascaris suum
1.1.1.39 R105A site-directed mutagenesis, fumarate binding residue, mutant shows 7-8fold reduced initial velocity with malate and Mg2+ compared to the wild-type enzyme, and is no longer activated by fumarate and malate Ascaris suum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.39 Mn2+ inhibits the reductive carboxylation reaction, inhibitory effect is about 20fold reduced by binding of fumarate and L-malate Ascaris suum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.39 additional information
-
 additional information detailed kinetic mechanism study, steady-state kinetics Ascaris suum

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.39 Mg2+ required Ascaris suum
1.1.1.39 Mn2+ required Ascaris suum
1.1.1.39 additional information the reaction is dependent on divalent metal ions Ascaris suum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.39 (S)-malate + NAD+ Ascaris suum
-
 pyruvate + CO2 + NADH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.39 Ascaris suum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.39 (S)-malate + NAD+
-
 Ascaris suum pyruvate + CO2 + NADH
-
 r

Synonyms

EC Number Synonyms Comment Organism
1.1.1.39 NAD-malic enzyme
-
 Ascaris suum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.39 25
-
 assay at Ascaris suum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.39 7
-
 assay at Ascaris suum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.39 NAD+
-
 Ascaris suum
1.1.1.39 NADH
-
 Ascaris suum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.39 additional information
-
 additional information
-
 Ascaris suum