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Literature summary extracted from

  • Oyedotun, K.S.; Lemire, B.D.
    The Saccharomyces cerevisiae succinate-ubiquinone oxidoreductase (1999), J. Biol. Chem., 274, 23956-23962.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.3.5.1 F103V the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Phe-103 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase, the enzyme is thermolabile at temperatures above 25°C Saccharomyces cerevisiae
1.3.5.1 H106L/D117V the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25°C Saccharomyces cerevisiae
1.3.5.1 H106Y the covalent FAD level is reduced, indicating some impairment of enzyme assembly, the quinone reductase activity is not greatly impaired, the enzyme is thermolabile at temperatures above 25°C Saccharomyces cerevisiae
1.3.5.1 H113Q the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, His-113 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase Saccharomyces cerevisiae
1.3.5.1 L122stop the covalent FAD level is reduced, indicating some impairment of enzyme assembly, quinone reductase activity is sharply reduced compared to wild-type, the enzyme is thermolabile at temperatures above 25°C Saccharomyces cerevisiae
1.3.5.1 W116R the covalent FAD level is not significantly different from the wild-type, the mutation strongly but specifically impairs quinone reductase activities but have only minor effects on enzyme assembly, Trp-116 in the Sdh3p subunit is important in the formation of a quinone-binding site in succinate dehydrogenase Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.5.1 2-alkyl-4,6-dinitrophenols complete inhibition of the wild-type enzyme and of the mutants H106Y and H113Q Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.5.1 0.0048
-
 2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone wild-type Saccharomyces cerevisiae
1.3.5.1 0.007
-
 2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone H106Y mutant Saccharomyces cerevisiae
1.3.5.1 0.0073
-
 2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone H106L/D117V mutant Saccharomyces cerevisiae
1.3.5.1 0.01
-
 2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone F103V mutant Saccharomyces cerevisiae
1.3.5.1 0.011
-
 2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone L122stop mutant Saccharomyces cerevisiae
1.3.5.1 0.015
-
 2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone H113Q mutant Saccharomyces cerevisiae
1.3.5.1 0.018
-
 2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone W116R mutant Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.5.1 succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone
-
 Saccharomyces cerevisiae fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol
-
 ?
1.3.5.1 succinate + ubiquinone
-
 Saccharomyces cerevisiae fumarate + ubiquinol
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.5.1 tetramer
-
 Saccharomyces cerevisiae