Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.39 extracted from

  • Aktas, D.F.; Cook, P.F.
    Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction (2008), Biochemistry, 47, 2539-2546.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
N434A site-directed mutagenesis, the interaction of the 434 position residue with malate is lost in the mutant, causing malate to reorient itself, leading to a slower decarboxylation Ascaris suum
N434E site-directed mutagenesis, the longer glutamine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme Ascaris suum
N434M site-directed mutagenesis, the longer methionine side chain sticks into the active site and causes a change in the position of malate and/or NAD+ resulting in more than a 10000fold decrease in V/Et for the mutant enzyme compared to the wild-type enzyme Ascaris suum
N479Q site-directed mutagenesis, the stepwise oxidative decarboxylation mechanism observed for the wild-type enzyme changed to a concerted one, which is totally rate limiting, for the N479Q mutant enzyme Ascaris suum
N479S site-directed mutagenesis, the mutant with the shorter serine side chain shows very similar values of KNAD+, Kmalate, and isotope effects relative to the wild-type enzyme, but V/Et is decreased 2000fold due to an increased freedom of rotation, resulting in nonproductively bound cofactor Ascaris suum
S433A site-directed mutagenesis, KNAD+ for the S433A mutant enzyme is increased by 80fold compared to the wild-type enzyme Ascaris suum
S433C site-directed mutagenesis, the mutant enzyme exhibits 9fold and 500fold increases in Kmalate and KNAD, respectively, compared to the wild-type enzyme Ascaris suum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information primary deuterium and 13C kinetic isotope effects, kinetics, and kinetic mechanism of wild-type and mutant enzymes, overview Ascaris suum
0.5
-
(S)-malate pH 7.0, 25°C, mutant N434A, in presence of Mn2+ Ascaris suum
0.8
-
NAD+ pH 7.0, 25°C, wild-type enzyme Ascaris suum
0.8
-
(S)-malate pH 7.0, 25°C, wild-type enzyme Ascaris suum
1.3
-
(S)-malate pH 7.0, 25°C, mutant S433A Ascaris suum
1.6
-
NAD+ pH 7.0, 25°C, mutant S433A Ascaris suum
1.7
-
NAD+ pH 7.0, 25°C, mutant N479S Ascaris suum
1.7
-
(S)-malate pH 7.0, 25°C, mutant N479S Ascaris suum
1.8
-
NAD+ pH 7.0, 25°C, mutant N479Q Ascaris suum
1.8
-
(S)-malate pH 7.0, 25°C, mutant N479Q Ascaris suum
2
-
NAD+ pH 7.0, 25°C, mutant N434A, in presence of Mn2+ Ascaris suum
2.2
-
(S)-malate pH 7.0, 25°C, mutant N434M Ascaris suum
3
-
NAD+ pH 7.0, 25°C, mutant N434M Ascaris suum
4.3
-
(S)-malate pH 7.0, 25°C, mutant N434Q Ascaris suum
5
-
NAD+ pH 7.0, 25°C, mutant N434Q Ascaris suum

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates mutant N434A 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
-
-
-

Reaction

Reaction Comment Organism Reaction ID
(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ acid-base chemical mechanism for Ascaris suum malic enzyme Ascaris suum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
Ascaris suum pyruvate + CO2 + NADH
-
r
(S)-malate + NAD+ the mitochondrial NAD-malic enzyme catalyzes the oxidative decarboxylation of malate to pyruvate and CO2 Ascaris suum pyruvate + CO2 + NADH
-
r

Synonyms

Synonyms Comment Organism
malic enzyme
-
Ascaris suum
mitochondrial 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+ binding structure, overview Ascaris suum
NADH
-
Ascaris suum