1.3.1.6: fumarate reductase (NADH)
This is an abbreviated version!
For detailed information about fumarate reductase (NADH), go to the full flat file.
Word Map on EC 1.3.1.6
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1.3.1.6
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nitrate
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malate
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shewanella
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fad
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flavoproteins
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fumarase
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iron-sulfur
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succinogenes
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ascaris
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flavocytochrome
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helminth
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oneidensis
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wolinella
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viologen
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anthelmintic
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frigidimarina
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succinate-ubiquinone
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tetraheme
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menaquinol
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narghji
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thiabendazole
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sdhcdab
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c4-dicarboxylate
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geobacter
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flavinylation
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succinate:quinone
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dmsabc
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hymenolepis
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cyma
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putrefaciens
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medicine
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drug development
- 1.3.1.6
- nitrate
- malate
- shewanella
- fad
- flavoproteins
- fumarase
-
iron-sulfur
- succinogenes
- ascaris
-
flavocytochrome
-
helminth
- oneidensis
-
wolinella
- viologen
-
anthelmintic
- frigidimarina
-
succinate-ubiquinone
-
tetraheme
- menaquinol
-
narghji
- thiabendazole
- sdhcdab
-
c4-dicarboxylate
- geobacter
-
flavinylation
-
succinate:quinone
- dmsabc
-
hymenolepis
-
cyma
- putrefaciens
- medicine
- drug development
Reaction
Synonyms
ABB37_00293, FRD, FRdABCD, FRDg, FRDm1, FRDm2, FRDS, Frds1p, fumarate reductase, KPA86010, KPK_2907, mitochondrial rhodoquinol-fumarate reductase, NADH-dependent fumarate reductase, NADH-FR, NADH-FRD, NADH-fumarate reductase, NFRD, QFR
ECTree
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Cofactor
Cofactor on EC 1.3.1.6 - fumarate reductase (NADH)
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FAD
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binding structure, FAD content of wild-type and mutant enzymes, overview
FAD
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flavoprotein subunit required for FRD activity, the subunit is phosphorylated for enzyme activity
FAD
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the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site
FAD
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the enzyme displays two redox active domains, one containing four c-type hemes and another containing FAD at the catalytic site
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enzyme contains 4 bis-His-ligated, c-type hemes, His61 is involved in binding, analysis of crystal structure, fumarate dependent reoxidation of the heme groups in mutants H61A and H61M are affected
heme
induces enzyme expression and is required for optimal anaerobic growth
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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
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tetraheme flavocytochrome c3
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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
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