Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.82 extracted from

  • Hirasawa, M.; Ruelland, E.; Schepens, I.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Knaff, D.B.
    Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast nicotinamide adenine dinucleotide phosphate-malate dehydrogenase (2000), Biochemistry, 39, 3344-3350.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information activation by light Sorghum bicolor
thioredoxin activates Sorghum sp.
thioredoxin the N-terminal disulfide formed between C24 and C29 has a more positive oxidation-reduction midpoint potential than the two other disulfides and is thus likely to be the preregulatory disulfide postulated to function in activating the enzyme Sorghum sp.

Protein Variants

Protein Variants Comment Organism
C24S/C207A oxidation-reduction midpoint potential is -310 mV at pH 7.0, compared to -330 mV for the wild-type enzyme Sorghum sp.
C24S/C29S oxidation-reduction midpoint potential is -280 mV at pH 7.0, compared to -330 mV for the wild-type enzyme Sorghum sp.

Localization

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

Organism

Organism UniProt Comment Textmining
Sorghum bicolor
-
-
-
Sorghum sp.
-
-
-

Substrates and Products (Substrate)

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