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Literature summary for 4.1.1.1 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 4.1.1.1

Inhibitors

Inhibitors Comment Organism Structure
additional information no inhibition by ferredoxin Pyrococcus furiosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information binding affinity of CoA is 0.11 mM Pyrococcus furiosus
1.1
-
 pyruvate pH and temperature not specified in the publication Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate 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), 60% at pH 10.2 (80°C) Pyrococcus furiosus acetaldehyde + CO2
-
 ?

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
-
 above Pyrococcus furiosus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
-
 Pyrococcus furiosus

pH Range

pH Minimum pH Maximum Comment Organism
8 11.5 pH 8.0: about 60% of maximal activity, pH 10.0: about 50% of maximal activity Pyrococcus furiosus

Cofactor

Cofactor Comment Organism Structure
CoA desulfocoenzyme A can substitute for CoA showing that the cofactor plays a structural rather than a catalytic role Pyrococcus furiosus