Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Smith, E.T.; Blamey, J.M.; Adams, M.W.
    Pyruvate ferredoxin oxidoreductases of the hyperthermophilic archaeon, Pyrococcus furiosus, and the hyperthermophilic bacterium, Thermotoga maritima, have different catalytic mechanisms (1994), Biochemistry, 33, 1008-1016.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.7.1 copper protein contains a copper-center Pyrococcus furiosus

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
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.1 additional information Incubation of the oxidized enzyme with CoA results in the partial reduction of a iron-sulfur center, which is not seen in the dithionite-reduced enzyme. Incubation of the oxidized enzyme with CoA results in the partial reduction of the copper site in POR. The addition of both pyruvate and CoA to the POR in its oxidized state results in the reduction of the same iron-sulfur center that is reduced by sodium dithionite Thermotoga maritima ?
-
 ?
1.2.7.1 additional information the addition of pyruvate to oxidized POR produces an isotropic signal centered at g = 2.01, assigned to a (hydroxyethy1)thiamine pyrophosphate radical intermediate. Incubation of the oxidized enzyme with CoA results in the partial reduction of the copper site in POR. The addition of both pyruvate and CoA to the POR in its oxidized state results in the reduction of the same iron-sulfur center that is reduced by sodium dithionite Pyrococcus furiosus ?
-
 ?
1.2.7.1 additional information Incubation of the oxidized enzyme with CoA results in the partial reduction of a iron-sulfur center, which is not seen in the dithionite-reduced enzyme. Incubation of the oxidized enzyme with CoA results in the partial reduction of the copper site in POR. The addition of both pyruvate and CoA to the POR in its oxidized state results in the reduction of the same iron-sulfur center that is reduced by sodium dithionite Thermotoga maritima DSM 3109 ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.7.1 80
-
-
 Thermotoga maritima
1.2.7.1 100
-
-
 Pyrococcus furiosus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.2.7.1 25
-
 inactive Thermotoga maritima
1.2.7.1 25
-
 inactive Pyrococcus furiosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.7.1 thiamine diphosphate
-
 Thermotoga maritima
1.2.7.1 thiamine diphosphate
-
 Pyrococcus furiosus
1.2.7.1 [4Fe-4S]-center protein contains at least two [4Fe-4S] ferredoxin-type clusters Thermotoga maritima
1.2.7.1 [4Fe-4S]-center protein contains at least two [4Fe-4S] ferredoxin-type clusters Pyrococcus furiosus