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Literature summary extracted from

  • Mueggler, P.A.; Wolfe, R.G.
    Malate dehydrogenase. Kinetic studies of substrate activation of supernatant enzyme by L-malate (1978), Biochemistry, 17, 4615-4620.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.37 L-malate
-
Sus scrofa
1.1.1.37 NADH product inhibition Sus scrofa
1.1.1.37 oxaloacetate
-
Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.37 0.036
-
oxaloacetate
-
Sus scrofa
1.1.1.37 0.14
-
NAD+
-
Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.37 mitochondrion
-
Sus scrofa 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.37 malate + NAD+ Sus scrofa
-
oxaloacetate + NADH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.37 Sus scrofa
-
pig
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.37
-
Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.37 heart
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.37 110
-
-
Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.37 (S)-malate + NAD+
-
Sus scrofa oxaloacetate + NADH + H+
-
r
1.1.1.37 malate + NAD+
-
Sus scrofa oxaloacetate + NADH + H+
-
r
1.1.1.37 oxaloacetate + NADH
-
Sus scrofa L-malate + NAD+
-
r

Subunits

EC Number Subunits Comment Organism
1.1.1.37 dimer
-
Sus scrofa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.37 76.7
-
L-malate
-
Sus scrofa