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Literature summary for 1.3.5.1 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
Search for more literature for 1.3.5.1

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
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
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
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
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
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
0.06
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
0.07
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
0.09
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
0.09
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
0.1
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
0.11
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
0.11
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
0.124
-
 reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
0.128
-
 reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli
0.13
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
0.13
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
0.14
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
0.15
-
 ubiquinone pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli
0.16
-
 ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
0.16
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
0.17
-
 reduced plumbagin pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli
0.19
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
0.2
-
 ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli

Localization

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
fumarate + reduced plumbagin
-
 Escherichia coli succinate + oxidized plumbagin
-
 ?
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 ?
-
 ?
succinate + ubiquinone
-
 Escherichia coli fumarate + ubiquinol
-
 ?
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

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.7
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
8.6
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
9.1
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
9.3
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
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
10.4
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
11.6
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHB mutant G227L Escherichia coli
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
12.7
-
 reduced plumbagin pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
15.6
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101L Escherichia coli
15.9
-
 reduced plumbagin pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli
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
16.2
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95L Escherichia coli
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
17.4
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHD mutant Q78L Escherichia coli
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
18.6
-
 ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli
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
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
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
20.9
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant E101D Escherichia coli
21.5
-
 reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
22.3
-
 ubiquinone pH 8.0, 25°C, recombinant subunit SDHC mutant D95E Escherichia coli
23
-
 reduced plumbagin pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95E Escherichia coli
24.8
-
 ubiquinone pH 7.0, 25°C, recombinant subunit SDHB/C mutant G227L/D95L Escherichia coli
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
37.9
-
 ubiquinone pH 8.0, 25°C, recombinant wild-type enzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Escherichia coli

Cofactor

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