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Literature summary for 1.3.1.6 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
Search for more literature for 1.3.1.6

KM Value [mM]

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Shewanella frigidimarina
-
-
-
Shewanella frigidimarina NCIMB400
-
-
-
Shewanella oneidensis
-
-
-
Shewanella oneidensis MR-1 / ATCC 700550
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms Comment Organism
fumarate reductase
-
 Shewanella oneidensis
fumarate reductase
-
 Shewanella frigidimarina

Cofactor

Cofactor Comment Organism Structure
FAD the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site Shewanella oneidensis
FAD the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site Shewanella frigidimarina
NAD+
-
 Shewanella oneidensis
NAD+
-
 Shewanella frigidimarina
NADH
-
 Shewanella oneidensis
NADH
-
 Shewanella frigidimarina
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
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

General Information

General Information Comment Organism
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
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