Protein Variants | Comment | Organism |
---|---|---|
C630A/R638A | naturally occuring mutant, overexpression of Sdh5 partially does not restore growth of the double mutant | Saccharomyces cerevisiae |
G70V/R638A | naturally occuring Sdh1 mutant, the mutant shows slightly reduced growth without glucose | Saccharomyces cerevisiae |
additional information | construction of several SDH subunit deletion strains, overview. Truncation of its last 13 residues of sdh1 abrogates this heme binding and renders the cells respiratory defective. Mutation of Arg638 compromises SDH function only when present in combination with a Cys630 substitution. Mutations of either Arg582 or Arg638/Cys630 do not markedly destabilize the Sdh1 polypeptide. The steady-state level of Sdh5 is markedly attenuated in the Sdh1 mutant cells | Saccharomyces cerevisiae |
R582A | site-directed mutagenesis, inactive mutant, no growth without glucose | Saccharomyces cerevisiae |
R582A/M599R | the mutant shows slightly reduced growth without glucose | Saccharomyces cerevisiae |
R582C | site-directed mutagenesis, the mutant shows slightly reduced growth without glucose | Saccharomyces cerevisiae |
R582W | naturally occuring mutant, inactive Sdh1 mutant | Saccharomyces cerevisiae |
R582W | site-directed mutagenesis, inactive mutant, no growth without glucose | Saccharomyces cerevisiae |
R638A | naturally occuring mutant, the mutant shows highly reduced growth without glucose, overexpression of Sdh5 partially restores growth of the single R638A mutant | Saccharomyces cerevisiae |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
70000 | - |
Sdh1 | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
SDH1 | - |
Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | FAD of Sdh1 is covalently attached at an active site His residue, 8alpha-N3-histidyl-FAD linkage, involving Arg582, required for enzyme activity. Flavinylation and assembly of succinate dehydrogenase are dependent on the C-terminal tail of the flavoprotein subunit. FAD binding is important to stabilize the Sdh1 conformation enabling association with Sdh2 and the membrane anchor subunits | Saccharomyces cerevisiae |