Literature summary for 1.1.1.38 extracted from

Rao, J.G.S.; Harris, B.G.; Cook, P.F.
Diethylpyrocarbonate inactivation of NAD-malic enzyme from Ascaris suum (1985), Arch. Biochem. Biophys., 241, 67-74.

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Inhibitors

Inhibitors	Comment	Organism	Structure
diethyldicarbonate	80% inactivation after treatment with 5 mM diethyldicarbonate for 25 min, biphasic inactivation, 40-50% inactivation in first phase, 1-2 histidine residues are acylated by diethyldicarbonate, 250 mM malate provides complete protection, 50% protection with 50 mM MgSO4, 55% enzyme activity is restored with 0.5 M hydroxylamine	Ascaris suum

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	-	-	-

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

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Ascaris suum

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Release 2023.1 (January 2023)