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Literature summary for 1.1.1.39 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

Activating Compound Comment Organism Structure
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
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)

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

Protein Variants

Protein Variants Comment Organism
K143A site-directed mutagenesis, malate binding residue, mutant shows highly increased kcat for malate and fumarate compared to the wild-type enzyme Ascaris suum
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

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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

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 pyruvate + CO2 + NADH
-
r

Synonyms

Synonyms Comment Organism
NAD-malic enzyme
-
Ascaris suum

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Ascaris suum
NADH
-
Ascaris suum

Ki Value [mM]

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