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Literature summary for 1.2.7.1 extracted from

  • Ma, K.; Hutchins, A.; Sung, S.J.; Adams, M.W.
    Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase (1997), Proc. Natl. Acad. Sci. USA, 94, 9608-9613.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.7.1

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
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Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA + 2 oxidized ferredoxin pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80°C (pH 8.0), the apparent Vm value for pyruvate decarboxylation is about 40% of the apparent Vm value for pyruvate oxidation rate (using Pyrococcus furiosus ferredoxin as the electron acceptor) Pyrococcus furiosus acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
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 ?

Synonyms

Synonyms Comment Organism
POR bifunctional enzyme that catalyzes both the oxidative and nonoxidative decarboxylation of pyruvate Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
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 Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
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 Pyrococcus furiosus

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8.5 pH 5.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity Pyrococcus furiosus