Literature summary for 1.1.1.82 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.

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Activating Compound

Activating Compound	Comment	Organism	Structure
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

General Stability	Organism
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

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

Organism

Organism	UniProt	Comment	Textmining
Pisum sativum	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
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

Source Tissue	Comment	Organism	Textmining
leaf	-	Pisum sativum	-

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)