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Literature summary for 1.1.1.82 extracted from

  • Krimm, I.; Goyer, A.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Lancelin, J.M.
    Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition (1999), J. Biol. Chem., 274, 34539-34542.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information activation by light Sorghum bicolor
additional information activation by light results from the thioredoxin-mediated reduction of two disulfides, located, respectively, in N- and C-terminal sequence extensions typical of all NADP-dependent light-regulated enzyme forms. The activation is a result of the unobstruction of the active site by acquisition of an additional mobility of the C-terminal 15-residue stretch Sorghum bicolor

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Sorghum bicolor 9507
-

Organism

Organism UniProt Comment Textmining
Sorghum bicolor
-
-
-

Substrates and Products (Substrate)

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