Literature summary extracted from

Scheibe, R.; Rudolph, R.; Reng, W.; Jaenicke, R.
Structural and catalytic properties of oxidized and reduced chloroplast NADP-malate dehydrogenase upon denaturation and renaturation (1990), Eur. J. Biochem., 189, 581-587.

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
1.1.1.82	additional information	in the absence of photosynthetic electron flow, the chloroplast enzyme exists in its disulfide-containing form which is inactive under physiological conditions. Upon interaction with reduced thioredoxin generated in the light, the active dithiol-containing enzyme is formed	Pisum sativum

General Stability

EC Number	General Stability	Organism
1.1.1.82	no effect of guanidine/HCl up to 0.25 M on the quarternary structure of the enzyme in its oxidized and reduced form. In the oxidized state the enzyme undergoes guanidine-dependent dissociation to the monomer with a midpoint of transition at 0.5 M. The kinetic of unfolding is significantly faster for the reduced than for the oxidized enzyme	Pisum sativum

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
1.1.1.82	chloroplast	-	Pisum sativum	9507	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.1.1.82	Pisum sativum	-	-	-

Renatured (Commentary)

EC Number	Renatured (Comment)	Organism
1.1.1.82	renaturation of the guanidine-HCl denatured enzyme is more rapid with the reduced enzyme and occurs with higher yields, 100%, than with the oxidized enzyme, 60-80%	Pisum sativum

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.1.1.82	leaf	-	Pisum sativum	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.1.1.82	oxaloacetate + NADPH	-	Pisum sativum	(S)-malate + NADP+	-	?

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Release 2023.1 (January 2023)