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Literature summary extracted from

  • Karsten, W.E.; Cook, P.F.
    Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum (2007), Biochemistry, 46, 14578-14588.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.39 R181K site-directed mutagenesis, the mutant shows a 100fold increase in the Km for malate, a 30fold increase in the Ki for oxalate, and a 10fold increase in Ki for NADH, but only a slight or no change in KNAD compared to the wild-type enzyme Ascaris suum
1.1.1.39 R181Q site-directed mutagenesis, the mutant shows a 100fold increase in the Km for malate, a 30fold increase in the Ki for oxalate, and a 10fold increase in Ki for NADH, but only a slight or no change in KNAD compared to the wild-type enzyme. The activity of the R181Q mutant can be partially rescued by ammonium ion likely by binding in the pocket vacated by the guanidinium group of R181 Ascaris suum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.39 oxalate very tight binding inhibitor of the NAD-malic enzyme 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 kinetics of wild-type and mutant enzymes, primary deuterium and 13C isotope effects of mutant R181Q in the absence and presence of ammonium ions, overview Ascaris suum
1.1.1.39 0.035
-
 NAD+ pH 8.5, 25°C, recombinant wild-type enzyme Ascaris suum
1.1.1.39 0.07
-
 NAD+ pH 8.5, 25°C, recombinant mutant R181Q Ascaris suum
1.1.1.39 0.53
-
 (S)-malate pH 8.5, 25°C, recombinant wild-type enzyme Ascaris suum
1.1.1.39 2 3 (S)-malate pH 8.5, 25°C, recombinant mutant R181Q in presence of 60 mM guanidinium Ascaris suum
1.1.1.39 8
-
 (S)-malate pH 8.5, 25°C, recombinant mutant R181Q, in presence of 60 mM NH4+ Ascaris suum
1.1.1.39 50
-
 (S)-malate pH 8.5, 25°C, recombinant mutant R181Q Ascaris suum
1.1.1.39 57
-
 (S)-malate pH 8.5, 25°C, recombinant mutant R181K Ascaris suum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.39 Mg2+
-
 Ascaris suum
1.1.1.39 NH4+ partially rescues the activity of the R181Q mutant by binding in the pocket vacated by the guanidinium group of R181, 2 mol of ammonia bind per mole of active sites, high-affinity Km is 0.7 mM, low-affinity Km is 420 mM 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
1.1.1.39 (S)-malate + NAD+ the NAD-malic enzyme catalyzes the oxidative decarboxylation of (S)-malate via oxaloacetate, Arg181 is within hydrogen bonding distance of the 1-carboxylate of malate in the active site of the enzyme and interacts with the carboxamide side chain of the nicotinamide ring of NADH, but not with 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, oxidation reaction Ascaris suum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.39 8.5
-
 assay at, oxidation reaction Ascaris suum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.39 additional information Arg181 is within hydrogen bonding distance of the 1-carboxylate of malate in the active site of the enzyme and interacts with the carboxamide side chain of the nicotinamide ring of NADH, but not with NAD+ Ascaris suum
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 inhibition patterns by measuring the initial rate as a function of malate or NAD+ with NAD+ or malate maintained equal to its Km at different fixed concentrations of oxalate, including zero, Ki, 2Ki, and 4Ki at pH 7.0 and 30 mM free Mg2+ Ascaris suum
1.1.1.39 0.006
-
 oxalate pH 7.0, 25°C, recombinant wild-type enzyme Ascaris suum