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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.82 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.82 50000 60000 unactivated enzyme, gel filtration Zea mays

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.82 Zea mays
-
-
-

Oxidation Stability

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.82
-
Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.82 leaf
-
Zea mays
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.82 160
-
-
Zea mays

Storage Stability

EC Number Storage Stability Organism
1.1.1.82 -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)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.82 7 8.5 activated enzyme Zea mays