Literature summary for 1.1.1.38 extracted from

Chooback, L.; Karsten, W.E.; Kulkarni, G.; Nalabolu, S.R.; Harris, B.G.; Cook, P.F.
Expression, purification, and characterization of the recombinant NAD-malic renzyme from Ascaris suum (1997), Protein Expr. Purif., 10, 51-54.

Search for more literature for 1.1.1.38

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Ascaris suum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.011	-	NAD+	native enzyme	Ascaris suum
0.015	-	NAD+	recombinant enzyme	Ascaris suum
1	-	L-malate	native enzyme	Ascaris suum
1.1	-	L-malate	recombinant enzyme	Ascaris suum

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Ascaris suum	5739	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(S)-malate + NAD+	Ascaris suum	-	CO2 + pyruvate + NADH	-	?
Oxaloacetate	Ascaris suum	-	CO2 + pyruvate	-	ir

Organism

Organism	UniProt	Comment	Textmining
Ascaris suum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
streptomycin sulfate ammonium sulfate, Phenyl-sepharose, Orange-A-Sepharose	Ascaris suum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
38.5	-	recombinant enzyme	Ascaris suum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-malate + NAD+	-	Ascaris suum	CO2 + pyruvate + NADH	-	?
(S)-malate + NAD+	-	Ascaris suum	CO2 + pyruvate + NADH	-	r
Oxaloacetate	-	Ascaris suum	CO2 + pyruvate	-	ir

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
130	-	L-malate	native and recombinant enzyme	Ascaris suum

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Ascaris suum

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Release 2023.1 (January 2023)