Cloned (Comment) | Organism |
---|---|
the encoding plasmid is transformed in Wolinella succinogenes | Wolinella succinogenes |
Protein Variants | Comment | Organism |
---|---|---|
A86H | FAD is non-covalently attached to SdhA. This is prooved by mutant A86H: in contrast to wild-tpye mutant A86H shows an additional fluorescent band which can be detected after SDS-PAGE | Wolinella succinogenes |
A86H | in wild-type enzyme FAD is non-covalenly-bound. In the enzyme containing a mutant A86H flavoprotein subunit the FAD is covalently bound | Wolinella succinogenes |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | the SdhABE complex is membrane associated rather than tightly membrane bound | Wolinella succinogenes | 16020 | - |
periplasm | in contrast to all other members of this superfamily, the enzyme is exported into the periplasm via the twin-arginine translocation (tat)-pathway | Wolinella succinogenes | - |
- |
periplasm | the hydrophilic subunits of the MFR complex are exported into the periplasm via the twin-arginine translocation (tat)-pathway | Wolinella succinogenes | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
fumarate + a menaquinol | Wolinella succinogenes | the enzyme is involved in anaerobic metabolism | succinate + a menaquinone | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | - |
- |
- |
Wolinella succinogenes | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Wolinella succinogenes |
a purification procedure is established to enrich the protein 24fold via a combination of anion exchange and gel filtration chromatography with a yield of 36% of the initial activity in the periplasm extract | Wolinella succinogenes |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
additional information | - |
enzyme shows no succinate oxidation activity but strong fumarate reduction activity | Wolinella succinogenes |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
fumarate + 8-methylmenaquinol-6 | - |
Wolinella succinogenes | succinate + 8-methylmenaquinone-6 | - |
? | |
fumarate + a menaquinol | the enzyme is involved in anaerobic metabolism | Wolinella succinogenes | succinate + a menaquinone | - |
? | |
additional information | fumarate reduction activity is measured by monitoring photometrically the oxidation of dithionite-reduced benzylviologen by fumarate | Wolinella succinogenes | ? | - |
? | |
additional information | succinate oxidation activity is determined using either methylene blue, dichlorophenolindophenol, ferricenium hexafluorophosphate, dimethylnaphthoquinone or as electron acceptor. Strikingly, no succinate oxidation activity is be detected, independent of the electron acceptor | Wolinella succinogenes | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
8-methylmenaquinol:fumarate reductase | - |
Wolinella succinogenes |
methylmenaquinol:fumarate reductase | - |
Wolinella succinogenes |
methylmenaquinol:fumarate reductase | - |
Campylobacter jejuni |
MFR | - |
Wolinella succinogenes |
MFR | - |
Campylobacter jejuni |
MFR complex | - |
Wolinella succinogenes |
MFR complex | - |
Campylobacter jejuni |
non-classical succinate:quinone reductase | - |
Wolinella succinogenes |
non-classical succinate:quinone reductase | - |
Campylobacter jejuni |
sdhABE | operon encoding for non-classical succinate quinone reductase | Wolinella succinogenes |
SQR | non-classical succinate quinone reductase | Wolinella succinogenes |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Wolinella succinogenes |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Wolinella succinogenes |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | FAD is non-covalently attached to SdhA. The reason for the lack of succinate oxidation activity might be explained by the absence of a covalently bound FAD which seems to be a prerequisite for succinate oxidation activity | Wolinella succinogenes | |
FAD | non-covalenly bound. In the enzyme containing a mutant A86H flavoprotein subunit the FAD is covalently bound | Wolinella succinogenes |
Organism | Comment | Expression |
---|---|---|
Campylobacter jejuni | sdhABE operon is upregulated in an oxygen-limited environment as compared with microaerophilic laboratory conditions | up |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is involved in anaerobic metabolism | Wolinella succinogenes |