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Literature summary extracted from

  • Juhnke, H.D.; Hiltscher, H.; Nasiri, H.R.; Schwalbe, H.; Lancaster, C.R.
    Production, characterization and determination of the real catalytic properties of the putative succinate dehydrogenase from Wolinella succinogenes (2009), Mol. Microbiol., 71, 1088-1101.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.5.1 the encoding plasmid is transformed in Wolinella succinogenes Wolinella succinogenes

Protein Variants

EC Number Protein Variants Comment Organism
1.3.5.1 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
1.3.5.1 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

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 membrane the SdhABE complex is membrane associated rather than tightly membrane bound Wolinella succinogenes 16020
-
1.3.5.1 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
-
-
1.3.5.1 periplasm the hydrophilic subunits of the MFR complex are exported into the periplasm via the twin-arginine translocation (tat)-pathway Wolinella succinogenes
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 fumarate + a menaquinol Wolinella succinogenes the enzyme is involved in anaerobic metabolism succinate + a menaquinone
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Campylobacter jejuni
-
-
-
1.3.5.1 Wolinella succinogenes
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.5.1
-
Wolinella succinogenes
1.3.5.1 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 [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.5.1 additional information
-
enzyme shows no succinate oxidation activity but strong fumarate reduction activity Wolinella succinogenes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 fumarate + 8-methylmenaquinol-6
-
Wolinella succinogenes succinate + 8-methylmenaquinone-6
-
?
1.3.5.1 fumarate + a menaquinol the enzyme is involved in anaerobic metabolism Wolinella succinogenes succinate + a menaquinone
-
?
1.3.5.1 additional information fumarate reduction activity is measured by monitoring photometrically the oxidation of dithionite-reduced benzylviologen by fumarate Wolinella succinogenes ?
-
?
1.3.5.1 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

EC Number Synonyms Comment Organism
1.3.5.1 8-methylmenaquinol:fumarate reductase
-
Wolinella succinogenes
1.3.5.1 methylmenaquinol:fumarate reductase
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Wolinella succinogenes
1.3.5.1 methylmenaquinol:fumarate reductase
-
Campylobacter jejuni
1.3.5.1 MFR
-
Wolinella succinogenes
1.3.5.1 MFR
-
Campylobacter jejuni
1.3.5.1 MFR complex
-
Wolinella succinogenes
1.3.5.1 MFR complex
-
Campylobacter jejuni
1.3.5.1 non-classical succinate:quinone reductase
-
Wolinella succinogenes
1.3.5.1 non-classical succinate:quinone reductase
-
Campylobacter jejuni
1.3.5.1 sdhABE operon encoding for non-classical succinate quinone reductase Wolinella succinogenes
1.3.5.1 SQR non-classical succinate quinone reductase Wolinella succinogenes

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.5.1 37
-
assay at Wolinella succinogenes

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.5.1 8
-
assay at Wolinella succinogenes

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 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
1.3.5.1 FAD non-covalenly bound. In the enzyme containing a mutant A86H flavoprotein subunit the FAD is covalently bound Wolinella succinogenes

Expression

EC Number Organism Comment Expression
1.3.5.1 Campylobacter jejuni sdhABE operon is upregulated in an oxygen-limited environment as compared with microaerophilic laboratory conditions up

General Information

EC Number General Information Comment Organism
1.3.5.1 physiological function the enzyme is involved in anaerobic metabolism Wolinella succinogenes