Cloned (Comment) | Organism |
---|---|
description of succinate dehydrogenase operon | Paracoccus denitrificans |
description of succinate dehydrogenase operon | Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
G168D | enzyme not assembled, properties of heme bP and heme bD seem normal | Bacillus subtilis |
H113L | enzyme not assembled | Bacillus subtilis |
H113M | assembled enzyme, low enzyme activity, altered properties of heme bD compared to wild-type | Bacillus subtilis |
H113Y | enzyme not assembled, contains heme | Bacillus subtilis |
H13Y | assembles enzyme with about 50% of normal activity, alters properties of heme bP and heme bD compared to wild-type, the isolated enzyme is not stable in the presence of succinate | Bacillus subtilis |
H155L | assembled enzyme, the enzyme has some activity but apparently is unstable | Bacillus subtilis |
H155Y | enzyme not assembled, contains heme | Bacillus subtilis |
H28L | assembles succinate dehydrogenase, active succinate dehydrogenase but inactive succinate: quinone reductase, contains heme bP but lacks low potential heme | Bacillus subtilis |
H28Y | enzyme not assembled, contains heme | Bacillus subtilis |
H47Y | assembles fully active enzyme | Bacillus subtilis |
H70L | enzyme not assembled | Bacillus subtilis |
H70Y | enzyme not assembled | Bacillus subtilis |
H70Y/Y73S | assembled enzyme, enzyme activity is 30% of normal | Bacillus subtilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-(n-heptyl)-4-hydroxy-quinoline N-oxide | potent inhibitor that affects both reduction and oxidation of quinone, the inhibitor binds close to heme bD | Bacillus subtilis | |
2-Thenoyltrifluoroacetone | - |
Paracoccus denitrificans | |
carboxin | not inhibitory | Bacillus subtilis | |
carboxin | interferes with electron transfer from the 3Fe-4S center to quinone, carboxin may bind to a quinone-binding site the Qp site, close to the 3Fe-4S center, amino acids involved in binding carboxin: a histidine residue in the B subunit and an aspartate residue in the D subunit | Paracoccus denitrificans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytoplasmic membrane | - |
Paracoccus denitrificans | - |
- |
cytoplasmic membrane | - |
Bacillus subtilis | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Paracoccus denitrificans | the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain | ? | - |
? | |
additional information | Bacillus subtilis | the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain | ? | - |
? | |
succinate + ubiquinone | Paracoccus denitrificans | - |
fumarate + ubiquinol | - |
? | |
succinate + ubiquinone | Bacillus subtilis | - |
fumarate + ubiquinol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
succinate dehydrogenase | - |
Paracoccus denitrificans | - |
succinate dehydrogenase | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain | Paracoccus denitrificans | ? | - |
? | |
additional information | the enzyme has the function to oxidize succinate to fumarate, as part of the Krebs' cycle and directly couples this to the reduction of quinone in the membrane, quinol is then oxidized by the respiratory chain | Bacillus subtilis | ? | - |
? | |
succinate + ubiquinone | - |
Paracoccus denitrificans | fumarate + ubiquinol | - |
? | |
succinate + ubiquinone | - |
Bacillus subtilis | fumarate + ubiquinol | - |
? | |
succinate + ubiquinone | electron acceptor: menaquinone | Bacillus subtilis | fumarate + ubiquinol | - |
? |
Subunits | Comment | Organism |
---|---|---|
tetramer | - |
Paracoccus denitrificans |
trimer | - |
Bacillus subtilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Paracoccus denitrificans | |
FAD | - |
Bacillus subtilis | |
heme b | - |
Paracoccus denitrificans | |
heme b | heme bP und heme bD | Bacillus subtilis | |
additional information | the enzyme contains iron-sulfur centers | Paracoccus denitrificans | |
additional information | the enzyme contains iron-sulfur centers | Bacillus subtilis |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0002 | - |
2-(n-heptyl)-4-hydroxy-quinoline N-oxide | - |
Bacillus subtilis |