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Literature summary for 1.1.1.40 extracted from

  • Ziegler, I.
    Malate dehydrogenase in Zea mays: properties and inhibition by sulfite (1974), Biochim. Biophys. Acta, 364, 28-37.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA
-
Zea mays
SO32- in decarboxylation of malate: partially competitive with respect to malate, in carboxylation of pyruvate: fully competitive for CO2 or HCO3- Zea mays
sulfite
-
Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
NADP+
-
Zea mays
0.045
-
NADPH
-
Zea mays
0.09
-
L-malate
-
Zea mays
3
-
pyruvate
-
Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required for decarboxylation of malate and decarboxylation of pyruvate, KM: 0.0018 mM Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
230000 240000 and a second molecular weight form of 460000-480000 Da, gel filtration Zea mays
460000 480000 and a second molecular weight form of 230000-240000 Da, gel filtration Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CO2 + NADPH
-
Zea mays L-malate + NADP+
-
r

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
carboxylation of pyruvate Zea mays
8
-
decarboxylation of malate Zea mays

Cofactor

Cofactor Comment Organism Structure
NADP+ cofactor Zea mays
NADPH cofactor Zea mays