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Literature summary for 1.3.5.1 extracted from

  • Yankovskaya, V.; Horsefield, R.; Tornroth, S.; Luna-Chavez, C.; Miyoshi, H.; Leger, C.; Byrne, B.; Cecchini, G.; Iwata, S.
    Architecture of succinate dehydrogenase and reactive oxygen species generation (2003), Science, 299, 700-704.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of SQR at 2.6 A resolution Escherichia coli
structure of SQR is reported at 2.6 A resolution. The SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of reactive oxygen species Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis Escherichia coli
360000
-
trimer 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
-
-
-
Escherichia coli P0AC41
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
trimer 3 * 120000 Da, SQR is packed as a trimer, determined by crystal structure analysis Escherichia coli

Synonyms

Synonyms Comment Organism
SQR
-
Escherichia coli
succinate dehydrogenase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD
-
Escherichia coli