Literature summary for 1.8.7.2 extracted from

Droux, M.; Miginiac-Maslow, M.; Jacquot, J.P.; Gadal, P.; Crawford, N.A.; Kosower, N.S.; Buchanan, B.B.
Ferredoxin-thioredoxin reductase: a catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation (1987), Arch. Biochem. Biophys., 256, 372-380.

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Organism

Organism	UniProt	Comment	Textmining
Spinacia oleracea	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Spinacia oleracea	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	FTR accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive disulfide to an active thiol form	Spinacia oleracea	?	-	?

Synonyms

Synonyms	Comment	Organism
FTR	-	Spinacia oleracea

General Information

General Information	Comment	Organism
physiological function	ferredoxin-thioredoxin reductase is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin m. The reduced thioredoxin m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive disulfide to an active thiol form	Spinacia oleracea

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Release 2023.1 (January 2023)