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Literature summary for 1.1.1.82 extracted from

  • Schepens, I.; Decottignies, P.; Ruelland, E.; Johansson, K.; Miginiac-Maslow, M.
    The dimer contact area of sorghum NADP-malate dehydrogenase: role of aspartate 101 in dimer stability and catalytic activity (2000), FEBS Lett., 471, 240-244.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
thioredoxin enzyme is activated by reduction of its N-terminal and C-terminal disulfides by reduced thioredoxin. The activation is inhibited by NADP+ Sorghum sp.

Protein Variants

Protein Variants Comment Organism
G84D 10fold lower Km for NADH, Km for NADPH remains unchanged Sorghum sp.
G84D/S851I/R87Q/S88A changed cofactor specificity from NADPH to NADH, the activation of the NAD-specific thiol-regulated enzyme is inhibited by NAD+ but no longer by NADP+ Sorghum sp.
S85I/R87Q/S88A 7fold increase in the Km-value for NADPH and 4fold decrease in Km-value for NADH Sorghum sp.

Localization

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

Organism

Organism UniProt Comment Textmining
Sorghum sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sorghum sp.

Substrates and Products (Substrate)

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