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 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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Ascaris suum | 5739 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | activates mutant N434A | Ascaris suum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NAD+ | Ascaris suum | - |
pyruvate + CO2 + NADH | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ascaris suum | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
(S)-malate + NAD+ = pyruvate + CO2 + NADH + H+ | acid-base chemical mechanism for Ascaris suum malic enzyme | Ascaris suum |
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 | Comment | Organism |
---|---|---|
malic enzyme | - |
Ascaris suum |
mitochondrial NAD-malic enzyme | - |
Ascaris suum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Ascaris suum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Ascaris suum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | binding structure, overview | Ascaris suum | |
NADH | - |
Ascaris suum |