BRENDA - Enzyme Database show

Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase

Ma, K.; Hutchins, A.; Sung, S.J.; Adams, M.W.; Proc. Natl. Acad. Sci. USA 94, 9608-9613 (1997)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.1.1.1
additional information
no inhibition by ferredoxin
Pyrococcus furiosus
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.1.1.1
additional information
-
additional information
binding affinity of CoA is 0.11 mM
Pyrococcus furiosus
4.1.1.1
1.1
-
pyruvate
pH and temperature not specified in the publication
Pyrococcus furiosus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.7.1
Pyrococcus furiosus
-
-
-
4.1.1.1
Pyrococcus furiosus
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.2.7.1
-
Pyrococcus furiosus
4.1.1.1
-
Pyrococcus furiosus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.7.1
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 80C (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)
723667
Pyrococcus furiosus
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
4.1.1.1
pyruvate
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80C (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 (80C)
723667
Pyrococcus furiosus
acetaldehyde + CO2
-
-
-
?
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
1.2.7.1
90
-
-
Pyrococcus furiosus
4.1.1.1
90
-
above
Pyrococcus furiosus
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.7.1
8
-
-
Pyrococcus furiosus
4.1.1.1
10
-
-
Pyrococcus furiosus
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.2.7.1
5.5
8.5
pH 5.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity
Pyrococcus furiosus
4.1.1.1
8
11.5
pH 8.0: about 60% of maximal activity, pH 10.0: about 50% of maximal activity
Pyrococcus furiosus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
4.1.1.1
CoA
desulfocoenzyme A can substitute for CoA showing that the cofactor plays a structural rather than a catalytic role
Pyrococcus furiosus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
4.1.1.1
CoA
desulfocoenzyme A can substitute for CoA showing that the cofactor plays a structural rather than a catalytic role
Pyrococcus furiosus
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.1.1.1
additional information
no inhibition by ferredoxin
Pyrococcus furiosus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.1.1.1
additional information
-
additional information
binding affinity of CoA is 0.11 mM
Pyrococcus furiosus
4.1.1.1
1.1
-
pyruvate
pH and temperature not specified in the publication
Pyrococcus furiosus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.7.1
-
Pyrococcus furiosus
4.1.1.1
-
Pyrococcus furiosus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.7.1
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 80C (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)
723667
Pyrococcus furiosus
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
4.1.1.1
pyruvate
pyruvate ferredoxin oxidoreductase functions as a CoA-dependent pyruvate decarboxylase. Ferredoxin is not necessary for the pyruvate decarboxylase activity of POR. At 80C (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 (80C)
723667
Pyrococcus furiosus
acetaldehyde + CO2
-
-
-
?
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
1.2.7.1
90
-
-
Pyrococcus furiosus
4.1.1.1
90
-
above
Pyrococcus furiosus
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.7.1
8
-
-
Pyrococcus furiosus
4.1.1.1
10
-
-
Pyrococcus furiosus
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
1.2.7.1
5.5
8.5
pH 5.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity
Pyrococcus furiosus
4.1.1.1
8
11.5
pH 8.0: about 60% of maximal activity, pH 10.0: about 50% of maximal activity
Pyrococcus furiosus