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Literature summary for 1.1.1.82 extracted from

  • Scheibe, R.; Wagenpfeil, D.; Fischer, J.
    NADP-malate dehydrogenase activity during photosynthesis in illuminated spinach chloroplasts (1986), J. Plant Physiol., 124, 103-110.
No PubMed abstract available
Search for more literature for 1.1.1.82

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
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 Spinacia oleracea 9507
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
oxaloacetate + NADPH Spinacia oleracea when no reoxidation of the light-generated NADPH can take place because of a lack of electron acceptors, full activation of the enzyme as well as reduction of thioredioxin m is observed. The fine regulation of the reductive activation of the enzyme determines the actual extent of export of reducing equivalents, in the form of malate, via the dicarboxylic acid translocator (S)-malate + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Spinacia oleracea
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + NADPH
-
 Spinacia oleracea (S)-malate + NADP+
-
 ?
oxaloacetate + NADPH when no reoxidation of the light-generated NADPH can take place because of a lack of electron acceptors, full activation of the enzyme as well as reduction of thioredioxin m is observed. The fine regulation of the reductive activation of the enzyme determines the actual extent of export of reducing equivalents, in the form of malate, via the dicarboxylic acid translocator Spinacia oleracea (S)-malate + NADP+
-
 ?