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Literature summary extracted from

  • Pessanha, M.; Rothery, E.L.; Miles, C.S.; Reid, G.A.; Chapman, S.K.; Louro, R.O.; Turner, D.L.; Salgueiro, C.A.; Xavier, A.V.
    Tuning of functional heme reduction potentials in Shewanella fumarate reductases (2009), Biochim. Biophys. Acta, 1787, 113-120.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.6 additional information
-
 additional information redox pattern and thermodynamics, overview Shewanella oneidensis
1.3.1.6 additional information
-
 additional information redox pattern and thermodynamics, overview Shewanella frigidimarina

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.6 periplasm
-
 Shewanella oneidensis
-
-
1.3.1.6 periplasm
-
 Shewanella frigidimarina
-
-
1.3.1.6 soluble
-
 Shewanella oneidensis
-
-
1.3.1.6 soluble
-
 Shewanella frigidimarina
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.6 succinate + NAD+ Shewanella oneidensis
-
 fumarate + NADH + H+
-
 r
1.3.1.6 succinate + NAD+ Shewanella frigidimarina
-
 fumarate + NADH + H+
-
 r
1.3.1.6 succinate + NAD+ Shewanella frigidimarina NCIMB400
-
 fumarate + NADH + H+
-
 r
1.3.1.6 succinate + NAD+ Shewanella oneidensis MR-1 / ATCC 700550
-
 fumarate + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.6 Shewanella frigidimarina
-
-
-
1.3.1.6 Shewanella frigidimarina NCIMB400
-
-
-
1.3.1.6 Shewanella oneidensis
-
-
-
1.3.1.6 Shewanella oneidensis MR-1 / ATCC 700550
-
-
-
1.3.5.1 Shewanella frigidimarina
-
 NCIMB400
-
1.3.5.1 Shewanella frigidimarina NCIMB400
-
 NCIMB400
-
1.3.5.1 Shewanella oneidensis
-
 MR-1
-
1.3.5.1 Shewanella oneidensis MR-1 / ATCC 700550
-
 MR-1
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.6 succinate + NAD+
-
 Shewanella oneidensis fumarate + NADH + H+
-
 r
1.3.1.6 succinate + NAD+
-
 Shewanella frigidimarina fumarate + NADH + H+
-
 r
1.3.1.6 succinate + NAD+
-
 Shewanella frigidimarina NCIMB400 fumarate + NADH + H+
-
 r
1.3.1.6 succinate + NAD+
-
 Shewanella oneidensis MR-1 / ATCC 700550 fumarate + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.3.1.6 monomer the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site Shewanella oneidensis
1.3.1.6 monomer the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site Shewanella frigidimarina

Synonyms

EC Number Synonyms Comment Organism
1.3.1.6 fumarate reductase
-
 Shewanella oneidensis
1.3.1.6 fumarate reductase
-
 Shewanella frigidimarina
1.3.5.1 fumarate reductase
-
 Shewanella oneidensis
1.3.5.1 fumarate reductase
-
 Shewanella frigidimarina

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.6 FAD the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site Shewanella oneidensis
1.3.1.6 FAD the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site Shewanella frigidimarina
1.3.1.6 NAD+
-
 Shewanella oneidensis
1.3.1.6 NAD+
-
 Shewanella frigidimarina
1.3.1.6 NADH
-
 Shewanella oneidensis
1.3.1.6 NADH
-
 Shewanella frigidimarina
1.3.1.6 tetraheme flavocytochrome c3 the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site. The redox behaviour of the fumarate reductase is similar and dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella oneidensis
1.3.1.6 tetraheme flavocytochrome c3 the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site. The redox behaviour of the fumarate reductase is similar and dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella frigidimarina
1.3.5.1 FAD proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella oneidensis
1.3.5.1 FAD proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella frigidimarina
1.3.5.1 heme proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella oneidensis
1.3.5.1 heme proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella frigidimarina

General Information

EC Number General Information Comment Organism
1.3.1.6 additional information the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site. The redox behaviour of the fumarate reductase is similar and dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella oneidensis
1.3.1.6 additional information the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site. The redox behaviour of the fumarate reductase is similar and dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV Shewanella frigidimarina