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Literature summary for 1.3.5.1 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
Search for more literature for 1.3.5.1

Cloned(Commentary)

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

Protein Variants

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Campylobacter jejuni
-
-
-
Wolinella succinogenes
-
-
-

Purification (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

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

pH Optimum

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

Cofactor

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

Expression

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

General Information

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