Protein Variants | Comment | Organism |
---|---|---|
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 |
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 |
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 |
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 |
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 |
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 | Comment | Organism | Structure |
---|---|---|---|
2-alkyl-4,6-dinitrophenols | complete inhibition of the wild-type enzyme and of the mutants H106Y and H113Q | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0048 | - |
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | wild-type | Saccharomyces cerevisiae | |
0.007 | - |
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | H106Y mutant | Saccharomyces cerevisiae | |
0.0073 | - |
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | H106L/D117V mutant | Saccharomyces cerevisiae | |
0.01 | - |
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | F103V mutant | Saccharomyces cerevisiae | |
0.011 | - |
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | L122stop mutant | Saccharomyces cerevisiae | |
0.015 | - |
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | H113Q mutant | Saccharomyces cerevisiae | |
0.018 | - |
2,3-Dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | W116R mutant | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
succinate dehydrogenase | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
succinate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone | - |
Saccharomyces cerevisiae | fumarate + 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinol | - |
? | |
succinate + ubiquinone | - |
Saccharomyces cerevisiae | fumarate + ubiquinol | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Saccharomyces cerevisiae |