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Literature summary for 1.1.1.82 extracted from

  • Jacquot, J.P.P.; Buchanan, B.B.; Martin, F.; Vidal, J.
    Enzyme regulation in C4 photosynthesis. Purification and properties of thioredoxin-linked NADP-malate dehydrogenase from corn leaves (1981), Plant Physiol., 68, 300-304.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
thioredoxin activated by thioredoxin m that is reduced either photochemically with ferredoxin and ferredoxin-thioredoxin reductase or chemically with dithiothreitol Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000 60000 unactivated enzyme, gel filtration Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Oxidation Stability

Oxidation Stability Organism
the enzyme undergoes reversible oxidation/reduction during its photoregulation Zea mays

Purification (Commentary)

Purification (Comment) Organism
-
 Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
160
-
-
 Zea mays

Storage Stability

Storage Stability Organism
-15°C, 37.5 mM Na-acetate, pH 5.5, 0.37 mM EDTA, 25% glycerol, no significant loss of activity after 3 months Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + NADH utilization of NADH to NADPH in reduction of oxaloacetate is 1:160 Zea mays (S)-malate + NAD+
-
 ?
oxaloacetate + NADPH
-
 Zea mays (S)-malate + NADP+
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5 activated enzyme Zea mays