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Literature summary for 1.1.1.82 extracted from

  • Braun, H.; Lichter, A.; Haberlein, I.
    Kinetic evidence for protein complexes between thioredoxin and NADP-malate dehydrogenase and presence of a thioredoxin binding site at the N-terminus of the enzyme (1996), Eur. J. Biochem., 240, 781-788.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thioredoxin activates Glycine max
thioredoxin thioredoxin/enzyme complex is an integral component of the thioredoxin mechanism responsible for the fine-tuning of the enzyme activity, the N-terminal 37 amino residues are involved in providing a specific thioredoxin binding-site Glycine max

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Glycine max
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Glycine max
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + NADPH
-
Glycine max (S)-malate + NADP+
-
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