1.3.8.12: (2S)-methylsuccinyl-CoA dehydrogenase
This is an abbreviated version!
For detailed information about (2S)-methylsuccinyl-CoA dehydrogenase, go to the full flat file.
Reaction
Synonyms
MCD, methylsuccinyl-CoA dehydrogenase, PdMCD
ECTree
1.3.8.12 (2S)-methylsuccinyl-CoA dehydrogenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.3.8.12 - (2S)-methylsuccinyl-CoA dehydrogenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
(2S)-methylsuccinyl-CoA + ferrocenium hexafluorophosphate
mesaconyl-CoA + ferricenium hexafluorophosphate
succinyl-CoA + electron-transfer flavoprotein
fumaryl-CoA + reduced electron-transfer flavoprotein
succinyl-CoA + ferrocenium hexafluorophosphate
fumaryl-CoA + ferricenium hexafluorophosphate
the enzyme shows about 0.5% activity with succinyl-CoA
-
-
?
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
the enzyme is involved ion the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
-
-
?
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
2-methylfumaryl-CoA + reduced 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
-
-
?
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein
2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
(2S)-methylsuccinyl-CoA + ferrocenium hexafluorophosphate
mesaconyl-CoA + ferricenium hexafluorophosphate
the enzyme is highly specific for (2S)-methylsuccinyl-CoA
-
-
?
(2S)-methylsuccinyl-CoA + ferrocenium hexafluorophosphate
mesaconyl-CoA + ferricenium hexafluorophosphate
the enzyme is highly specific for (2S)-methylsuccinyl-CoA
-
-
?
succinyl-CoA + electron-transfer flavoprotein
fumaryl-CoA + reduced electron-transfer flavoprotein
low activity
-
-
?
succinyl-CoA + electron-transfer flavoprotein
fumaryl-CoA + reduced electron-transfer flavoprotein
low activity
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
the enzyme has no detectable activity toward (2R)-methylsuccinyl-CoA, butyryl-CoA, and isobutyryl-CoA
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
the enzyme has no detectable activity toward (2R)-methylsuccinyl-CoA, butyryl-CoA, and isobutyryl-CoA
-
-
-
