Protein Variants | Comment | Organism |
---|---|---|
N434A | with N434A, the interaction of the residue with malate is lost, causing the malate to reorient itself, leading to a slower decarboxylation step | Ascaris suum |
N479Q | the Kmalate value for the N479Q mutant enzyme increases by 2.2fold compared to the wild type enzyme, the KNAD value for the N479Q mutant enzyme increases by 1.1fold compared to the wild type enzyme | Ascaris suum |
N479S | the Kmalate value for the N479Q mutant enzyme increases by 2.1fold compared to the wild type enzyme, the KNAD value for the N479Q mutant enzyme increases by 1.8fold compared to the wild type enzyme | Ascaris suum |
S433A | the KNAD value for the S433A mutant enzyme increases by 80fold compared to the wild type enzyme, indicating that this residue provides significant binding affinity for the dinucleotide | Ascaris suum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Ascaris suum | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Ascaris suum | P27443 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NAD+ | - |
Ascaris suum | CO2 + pyruvate + NADH | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MHD | - |
Ascaris suum |
mitochondrial NAD-malic enzyme | - |
Ascaris suum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Ascaris suum |