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
1.3.1.6 fumarate reductase (NADH)Advanced search results
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Engineering on EC 1.3.1.6 - fumarate reductase (NADH)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S9N
Ser9 replacement abolishes the flavinylation and fumarate reductase activity of FRD
H505A
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site-directed mutagenesis, altered binding structure of the sodium ion, crystal structure analysis, at pH 8.5 the activity of the mutant enzyme is similar to the wild-type enzyme, at pH 6.0 the ctivity is 20fold reduced
H505Y
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site-directed mutagenesis, altered binding structure of the sodium ion, crystal structure analysis, at pH 8.5 the activity of the mutant enzyme is similar to the wild-type enzyme
H61A
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site-directed mutagenesis, 5-10fold reduced kcat compared to the wild-type enzyme, elevated pH optimum, electrochemical analysis, crystal structure analysis, altered ligand binding of hemes and heme iron, 80% of wild-type activity can be recovered by addition of exogenous imidazole, overview
H61M
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site-directed mutagenesis, 5-10fold reduced kcat compared to the wild-type enzyme, elevated pH optimum, electrochemical analysis, crystal structure analysis, altered ligand binding of hemes and heme iron, 80% of wild-type activity can be recovered by addition of exogenous imidazole, overview
additional information
additional information
construction of in frame-deletions mutants of frdC and frdB, mutation results in mutants with no catalytic activity and threefold increased generation time compared to the wild-type strain, growth can partially be restored by addition of succinate to the medium
additional information
construction of in frame-deletions mutants of frdC and frdB, mutation results in mutants with no catalytic activity and threefold increased generation time compared to the wild-type strain, growth can partially be restored by addition of succinate to the medium
additional information
construction of in frame-deletions mutants of frdC and frdB, mutation results in mutants with no catalytic activity and threefold increased generation time compared to the wild-type strain, growth can partially be restored by addition of succinate to the medium
additional information
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construction of in frame-deletions mutants of frdC and frdB, mutation results in mutants with no catalytic activity and threefold increased generation time compared to the wild-type strain, growth can partially be restored by addition of succinate to the medium
additional information
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construction of gene disruption mutants, simultaneous disruption of genes FRDS and OSM1 cause a growth defect mutant under anaerobic conditions, while disruption of gene OSM1 alone leads to a slow growth, both due to lack in cellular NAD+, which can be overcome by addition of methylene blue or phenazine methosulfate which oxidized NADH to NAD+
additional information
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DELTAfrdABCD mutant (fumarate reductase) is deficient in the ability to run the reductive branch of the tricarboxylic acid cycle, fumarate reductase can replace succinate dehydrogenase by running in the same direction as succinate dehydrogenase in order to run a full tricarboxylic acid cycle
