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Literature summary extracted from
- The Saccharomyces cerevisiae succinate dehydrogenase does not require heme for ubiquinone reduction (2007), Biochim. Biophys. Acta, 1767, 1436-1445.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.3.5.1 | complementation of a commercially available SDH3/SDH4 double knockout mutant yeast strain, subcloning of SDH genes in Escherichia coli strain DH5alpha | Saccharomyces cerevisiae |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | C78A | site-directed mutagenesis of the subunit Sdh4p residue an axial ligand of heme binding, leads to highly reduced to undetectable levels of heme b562 compared to the wild-type enzyme | Saccharomyces cerevisiae |
| 1.3.5.1 | C78A/H106A | site-directed mutagenesis of the subunits Sdh3p and Sdh4p, leads to highly reduced to undetectable levels of heme b562 and reduced cell growth compared to the wild-type enzyme | Saccharomyces cerevisiae |
| 1.3.5.1 | H106A | site-directed mutagenesis of the subunit Sdh3p residue, an axial ligand of heme binding, leads to highly reduced to undetectable levels of heme b562 compared to the wild-type enzyme | Saccharomyces cerevisiae |
| 1.3.5.1 | additional information | construction of a gene SDH3 disruption mutant by gene replacement, effects of mutations of the enzyme subunits on the electron transfer activities in mitochondrial membranes of mutant yeast cells compared to the wild-type strain, overview | Saccharomyces cerevisiae |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.3.5.1 | 0.003 | - |
2,6-dichlorophenol indophenol | 22°C, wild-type strain YPH499 | Saccharomyces cerevisiae |  |
| 1.3.5.1 | 0.007 | - |
2,6-dichlorophenol indophenol | 22°C, Sdh3p/Sdh4p double mutant strain H106A/C78A | Saccharomyces cerevisiae | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.3.5.1 | mitochondrial membrane | the enzyme has a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview | Saccharomyces cerevisiae | 31966 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.5.1 | Fe2+ | non-heme iron in the iron-sulfur protein in subunit Sdh2p as part of the catalytic dimer of the tetrameric enzyme, and heme iron in a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview | Saccharomyces cerevisiae | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.5.1 | succinate + ubiquinone | Saccharomyces cerevisiae | - |
fumarate + ubiquinol | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.3.5.1 | Saccharomyces cerevisiae | - |
wild-type strain YPH499 | - |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.3.5.1 | additional information | - |
- |
Saccharomyces cerevisiae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.3.5.1 | succinate + 2,6-dichlorophenol indophenol | - |
Saccharomyces cerevisiae | fumarate + reduced 2,6-dichlorophenol indophenol | - |
? | |
| 1.3.5.1 | succinate + ubiquinone | - |
Saccharomyces cerevisiae | fumarate + ubiquinol | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | More | structure molecular dynamic simulations using the crystal structure with PDB ID 1PB4 | Saccharomyces cerevisiae |
| 1.3.5.1 | tetramer | composed of a catalytic dimer, comprising a flavoprotein subunit Sdh1p and an iron-sulfur protein Sdh2p, and a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview | Saccharomyces cerevisiae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.3.5.1 | SDH | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.3.5.1 | 22 | - |
assay at | Saccharomyces cerevisiae |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.3.5.1 | FAD | flavoprotein, 41 pmol FAD per mg of protein in wild-type strain YPH499, possesses a flavoprotein subunit Sdh1p as part of the catalytic dimer of the tetrameric enzyme | Saccharomyces cerevisiae | |
| 1.3.5.1 | heme b562 | the enzyme has a heme b-containing membrane-anchoring dimer, comprising the Sdh3p and Sdh4p subunits, overview | Saccharomyces cerevisiae | |
| 1.3.5.1 | ubiquinone | - |
Saccharomyces cerevisiae | |
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Release 2023.1 (January 2023)
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