Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Silkin, Y.; Oyedotun, K.S.; Lemire, B.D.
    The role of Sdh4p Tyr-89 in ubiquinone reduction by the Saccharomyces cerevisiae succinate dehydrogenase (2006), Biochim. Biophys. Acta, 1767, 143-150.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.5.1 membrane bound Saccharomyces cerevisiae 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.5.1 Fe-S cluster two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
1.3.5.1 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 succinate + ubiquinone two electrons from succinate are transferred one at a time through a flavin cofactor and a chain of iron-sulfur clusters to reduce ubiquinone to an ubisemiquinone intermediate and to ubiquinol, role of Tyr-89 in the protonation of ubiquinone Saccharomyces cerevisiae fumarate + ubiquinol
-
?