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Literature summary extracted from

  • Kletzin, A.; Adams, M.W.W.
    Molecular and phylogenetic chararcterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima (1996), J. Bacteriol., 178, 248-257.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.7.7 thiamine diphosphate requires for maximal activity of enzyme Pyrococcus furiosus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.7.7
-
 Pyrococcus furiosus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.7.7 Fe each of the tetramer contains three [4Fe-4S] cluster Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.7.7 11851
-
 alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences Pyrococcus furiosus
1.2.7.7 20033
-
 alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences Pyrococcus furiosus
1.2.7.7 34766
-
 alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences Pyrococcus furiosus
1.2.7.7 43960
-
 alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences Pyrococcus furiosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.7.7 additional information Pyrococcus furiosus enzyme catalyses the CoA-dependent oxidation of branched-chain 2-ketoacids ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.1 Pyrococcus furiosus Q51804 and Q51805 and Q51803 and Q51799 Q51804 i.e. subunit PorA, Q51805 i.e. subunit PorB, Q51803 i.e. subunit PorD, Q51799 i.e. subunit PorG
-
1.2.7.1 Thermotoga maritima O05651 and Q56317 and O05650 and Q56316 O05651 i.e. subunit PorA, Q56317 i.e. subunit PorB, O05650 i.e. subunit PorC, Q56316 i.e. subunit PorD
-
1.2.7.1 Thermotoga maritima DSM 3109 O05651 and Q56317 and O05650 and Q56316 O05651 i.e. subunit PorA, Q56317 i.e. subunit PorB, O05650 i.e. subunit PorC, Q56316 i.e. subunit PorD
-
1.2.7.7 Pyrococcus furiosus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.2.7.7 3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + 2 reduced ferredoxin + 2 H+ this enzyme is one of four 2-oxoacid oxidoreductases: indolepyruvate oxidoreductase, EC 1.2.7.8, pyruvate oxidoreductase, EC 1.2.7.1., 2-oxogluterate oxidoreductase, EC 1.2.7.3 Pyrococcus furiosus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.7 additional information enzyme catalyses the CoA-dependent oxidation of branched-chain 2-ketoacids Pyrococcus furiosus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.2.7.7 ? alpha,beta,gamma,delta, x * 43960 + x * 34766 + x * 20033 + x * 11851, SDS PAGE, amino acid sequences Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.7.1 thiamine diphosphate the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain Thermotoga maritima
1.2.7.1 thiamine diphosphate the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain Pyrococcus furiosus
1.2.7.1 [4Fe-4S]-center the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP Thermotoga maritima
1.2.7.1 [4Fe-4S]-center the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP Pyrococcus furiosus

Expression

EC Number Organism Comment Expression
1.2.7.1 Pyrococcus furiosus the operon organization for Pyrococcus furiosus pyruvate ferredoxin oxidoreductase POR and 2-oxoisovalerate ferredoxin oxidoreductase VOR is porG-vorDAB-porDAB, wherein the gamma subunit is shared by the two enzymes additional information