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Literature summary for 1.3.5.1 extracted from

  • Tornroth, S.; Yankovskaya, V.; Cecchini, G.; Iwata, S.
    Purification, crystallisation and preliminary crystallographic studies of succinate:ubiquinone oxidoreductase from Escherichia coli (2002), Biochim. Biophys. Acta, 1553, 171-176.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
transformed strain DW35 used for expression of membrane-bound enzyme Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
by the hanging-drop vapour-diffusion technique Escherichia coli

Localization

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
succinate dehydrogenase
-

Purification (Commentary)

Purification (Comment) Organism
using treatment with detergent Thesit and chromatography on DEAE-Sepharose FF column, Poros 50HQ column and Sephacryl S-300 gel filtration column Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
90 100 succinate
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
cytochrome b succinate dehydrogenase contains one heme b Escherichia coli