Literature summary for 1.2.7.1 extracted from

Pieulle, L.; Stocker, P.; Vinay, M.; Nouailler, M.; Vita, N.; Brasseur, G.; Garcin, E.; Sebban-Kreuzer, C.; Dolla, A.
Study of the thiol/disulfide redox systems of the anaerobe Desulfovibrio vulgaris points out pyruvate:ferredoxin oxidoreductase as a new target for thioredoxin 1 (2011), J. Biol. Chem., 286, 7812-7821.

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Activating Compound

Activating Compound	Comment	Organism	Structure
thioredoxin 1	the Desulfovibrio vulgaris thioredoxin1 system activates the enzyme	Desulfovibrio vulgaris

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
pyruvate + CoA + oxidized ferredoxin	Desulfovibrio vulgaris	-	acetyl-CoA + CO2 + reduced ferredoxin + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Desulfovibrio vulgaris	-	-	-

Oxidation Stability

Oxidation Stability	Organism
the enzyme is efficiently protected when cells are exposed to air or H2O2	Desulfovibrio vulgaris

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
pyruvate + CoA + oxidized ferredoxin	-	Desulfovibrio vulgaris	acetyl-CoA + CO2 + reduced ferredoxin + H+	-	?

Synonyms

Synonyms	Comment	Organism
PFOR	-	Desulfovibrio vulgaris
pyruvate:ferredoxin oxidoreductase	-	Desulfovibrio vulgaris

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Release 2023.1 (January 2023)