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Literature summary extracted from

  • Cheng, V.W.; Johnson, A.; Rothery, R.A.; Weiner, J.H.
    Alternative sites for proton entry from the cytoplasm to the quinone binding site in Escherichia coli succinate dehydrogenase (2008), Biochemistry, 47, 9107-9116.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.5.1 expression of wild-type and mutant enzymes in strain DW35 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.3.5.1 D95E site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme Escherichia coli
1.3.5.1 D95L site-directed mutagenesis of subunit C, the mutant shows a shifted pH-optimum but similar activity compared to the wild-type enzyme Escherichia coli
1.3.5.1 E101D site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme Escherichia coli
1.3.5.1 E101L site-directed mutagenesis of subunit C, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme Escherichia coli
1.3.5.1 G227L site-directed mutagenesis of subunit B, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme Escherichia coli
1.3.5.1 G227L/D95E site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0 Escherichia coli
1.3.5.1 G227L/D95L site-directed mutagenesis of subunits B and C, respectively, the mutant shows a shifted pH optimum compared to the wild-type enzyme and is inactive above pH 7.0 Escherichia coli
1.3.5.1 Q78L site-directed mutagenesis of subunit D, the mutant shows reduced activity and a shifted pH-optimum compared to the wild-type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.5.1 additional information
-
additional information midpoint potentials of [3Fe-4S] cluster and heme b, kinetics and kinetic isotope effects of recombinant wild-type and mutant enzymes at different pH in both reaction directions, overview Escherichia coli
1.3.5.1 0.06
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
1.3.5.1 0.07
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
1.3.5.1 0.09
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
1.3.5.1 0.09
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
1.3.5.1 0.1
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
1.3.5.1 0.11
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
1.3.5.1 0.11
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
1.3.5.1 0.124
-
reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
1.3.5.1 0.128
-
reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli
1.3.5.1 0.13
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
1.3.5.1 0.13
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
1.3.5.1 0.14
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
1.3.5.1 0.15
-
ubiquinone pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli
1.3.5.1 0.16
-
ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
1.3.5.1 0.16
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
1.3.5.1 0.17
-
reduced plumbagin pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli
1.3.5.1 0.19
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
1.3.5.1 0.2
-
ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 membrane
-
Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.5.1 Fe2+ heme cofactor and [3Fe-4S] cluster, midpoint potentials of wild-type and mutant enzymes, overview Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.5.1 succinate + ubiquinone Escherichia coli
-
fumarate + ubiquinol
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.5.1 recombinant wild-type and mutant enzymes partially from strain DW35 by membrane preparation Escherichia coli

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.5.1 additional information aerobic growth on succinate and anaerobic growth on glycerol-fumarate Escherichia coli
-

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
-
catalytic efficiencies of recombinant wild-type and mutant enzymes at different pH in both reaction directions, overview Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 fumarate + reduced plumbagin
-
Escherichia coli succinate + oxidized plumbagin
-
?
1.3.5.1 succinate + 2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide i.e. MTT, in presence of phenazine methosulfate, i.e. PMS Escherichia coli ?
-
?
1.3.5.1 succinate + ubiquinone
-
Escherichia coli fumarate + ubiquinol
-
?
1.3.5.1 succinate + ubiquinone the enzyme does not generate a proton motive force during catalysis and are electroneutral, thus, the quinone reduction reaction must consume cytoplasmic protons which are released stoichiometrically during succinate oxidation. Residues SdhBG227, SdhCD95, and SdhCE101 are located at or near the entrance of a water channel that functions as a proton wire connecting the cytoplasm to the quinone binding site in vivo, while an alternative proton pathway exists in vitro only, overview Escherichia coli fumarate + ubiquinol
-
?

Synonyms

EC Number Synonyms Comment Organism
1.3.5.1 More SDH belongs to the highly conserved complex II family of enzymes that reduce ubiquinone Escherichia coli
1.3.5.1 SDH
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.5.1 25
-
assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.5.1 7.7
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
1.3.5.1 8.6
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
1.3.5.1 9.1
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
1.3.5.1 9.3
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
1.3.5.1 9.4
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
1.3.5.1 10.4
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
1.3.5.1 11.6
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
1.3.5.1 12.6
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
1.3.5.1 12.7
-
reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
1.3.5.1 15.6
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
1.3.5.1 15.9
-
reduced plumbagin pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli
1.3.5.1 15.9
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
1.3.5.1 16.2
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
1.3.5.1 17.4
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
1.3.5.1 17.4
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
1.3.5.1 18
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
1.3.5.1 18.6
-
ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli
1.3.5.1 19.9
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli
1.3.5.1 20.8
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
1.3.5.1 20.9
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli
1.3.5.1 20.9
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
1.3.5.1 21.5
-
reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
1.3.5.1 22.3
-
ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
1.3.5.1 23
-
reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli
1.3.5.1 24.8
-
ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
1.3.5.1 29.6
-
2-(4,5-dimethyl-2-thiazolyl)-3,5-diphenyl-2H-tetrazolium bromide pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
1.3.5.1 37.9
-
ubiquinone pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.5.1 8
-
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.5.1 flavin quantitative determination of content in wild-type and mutant enzymes Escherichia coli
1.3.5.1 heme a single heme b moiety is incorporated into the membrane anchor and only the QP-site is functional Escherichia coli
1.3.5.1 Plumbagin a quinone analogue Escherichia coli
1.3.5.1 quinone with a periplasmically oriented quinone binding site of the enzyme Escherichia coli