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Literature summary for 1.1.1.82 extracted from

  • Ferte, N.; Meunier, J.C.
    Purification of several NADP-dependent malate dehydrogenase isoenzymes from spinach leaves. Kinetic properties (1984), Plant Sci. Lett., 37, 115-121.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
malate
-
Spinacia oleracea
NADP+
-
Spinacia oleracea
NADPH substrate inhibition Spinacia oleracea
oxaloacetate substrate inhibition Spinacia oleracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.11
-
oxaloacetate
-
Spinacia oleracea
0.36
-
NADPH
-
Spinacia oleracea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
57000
-
equilibrium sedimentation Spinacia oleracea

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Purification (Commentary)

Purification (Comment) Organism
4 isoenzymes Spinacia oleracea

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Spinacia oleracea
-

Substrates and Products (Substrate)

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