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Literature summary for 1.1.1.38 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
Search for more literature for 1.1.1.38

Protein Variants

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

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

Organism

Organism UniProt Comment Textmining
Ascaris suum P27443
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
 Ascaris suum CO2 + pyruvate + NADH
-
 ?

Synonyms

Synonyms Comment Organism
MHD
-
 Ascaris suum
mitochondrial NAD-malic enzyme
-
 Ascaris suum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Ascaris suum