Literature summary for 1.1.1.37 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.

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Inhibitors

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

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	pig	-

Purification (Commentary)

Purification (Comment)	Organism
-	Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
heart	-	Sus scrofa	-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
dimer	-	Sus scrofa

Turnover Number [1/s]

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

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Release 2023.1 (January 2023)