EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   1.3.8.12 | (2S)-methylsuccinyl-CoA + electron-transfer flavoprotein |
- |
Cereibacter sphaeroides |
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein |
- |
? |
| 1.3.8.12 | (2S)-methylsuccinyl-CoA + electron-transfer flavoprotein |
- |
Paracoccus denitrificans |
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein |
- |
? |
| 1.3.8.12 | (2S)-methylsuccinyl-CoA + electron-transfer flavoprotein |
the enzyme is involved ion the ethylmalonyl-CoA pathway for acetyl-CoA assimilation |
Cereibacter sphaeroides |
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein |
- |
? |
| 1.3.8.12 | (2S)-methylsuccinyl-CoA + electron-transfer flavoprotein |
the enzyme is highly specific for (S)-methylsuccinyl-CoA. No activity with butyryl-CoA, isobutyryl-CoA or a diastereomeric mixture of (R)-methylsuccinyl-CoA |
Cereibacter sphaeroides |
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein |
- |
? |
| 1.3.8.12 | (2S)-methylsuccinyl-CoA + electron-transfer flavoprotein |
- |
Paracoccus denitrificans Pd1222 |
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein |
- |
? |
| 1.3.8.12 | (2S)-methylsuccinyl-CoA + ferrocenium hexafluorophosphate |
the enzyme is highly specific for (2S)-methylsuccinyl-CoA |
Paracoccus denitrificans |
mesaconyl-CoA + ferricenium hexafluorophosphate |
- |
? |
| 1.3.8.12 | (2S)-methylsuccinyl-CoA + ferrocenium hexafluorophosphate |
the enzyme is highly specific for (2S)-methylsuccinyl-CoA |
Paracoccus denitrificans Pd1222 |
mesaconyl-CoA + ferricenium hexafluorophosphate |
- |
? |
| 1.3.8.12 | more |
FAD does not dissociate from the enzyme during catalysis. The reaction product can only be released after FAD is re-oxidized within the active site by a final electron acceptor |
Cereibacter sphaeroides |
? |
- |
- |
| 1.3.8.12 | more |
substrate specificity of methylsuccinyl-CoA dehydrogenase, structure-function analysis, overview. The enzyme catalyzes the oxidation of (2S)-methylsuccinyl-CoA to alpha,beta-unsaturated mesaconyl-CoA and shows only about 0.5% activity with succinyl-CoA. MCD catalyzes the unprecedented oxidation of an alpha-methyl branched dicarboxylic acid CoA thioester. Substrate specificity is achieved by a cluster of three arginines that accommodates the terminal carboxyl group and a dedicated cavity that facilitates binding of the C2 methyl branch. The alpha,beta-desaturation of the CoA thioester is initiated by a proton abstraction from the alpha-carbon by a conserved catalytically active glutamate and a hydride transfer from the beta-carbon to the N5 of the FAD cofactor. The reduced cofactor is reoxidized by two sequential one-electron transfers to electron transfer flavoproteins (ETFs), which in turn deliver the electrons to the membrane-bound electron transport chain for energy conservation |
Paracoccus denitrificans |
? |
- |
- |
| 1.3.8.12 | more |
the enzyme has no detectable activity toward (2R)-methylsuccinyl-CoA, butyryl-CoA, and isobutyryl-CoA |
Paracoccus denitrificans |
? |
- |
- |
