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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
periplasm | - |
Shewanella oneidensis | - |
- |
periplasm | - |
Shewanella frigidimarina | - |
- |
soluble | - |
Shewanella oneidensis | - |
- |
soluble | - |
Shewanella frigidimarina | - |
- |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Shewanella frigidimarina | - |
- |
- |
Shewanella frigidimarina NCIMB400 | - |
- |
- |
Shewanella oneidensis | - |
- |
- |
Shewanella oneidensis MR-1 / ATCC 700550 | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
fumarate reductase | - |
Shewanella oneidensis |
fumarate reductase | - |
Shewanella frigidimarina |
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 | 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 |