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EC Tree
IUBMB Comments The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. The enzyme contains FAD.
The enzyme appears in viruses and cellular organisms
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(2S)-methylsuccinyl-CoA + electron-transfer flavoprotein = 2-methylfumaryl-CoA + reduced electron-transfer flavoprotein
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(2S)-methylsuccinyl-CoA:electron-transfer flavoprotein oxidoreductase
The enzyme, characterized from the bacterium Rhodobacter sphaeroides, is involved in the ethylmalonyl-CoA pathway for acetyl-CoA assimilation. The enzyme contains FAD.
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(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
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(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
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(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
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FAD
the enzyme contains 0.7 mol of noncovalently bound FAD molecule per subunit
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UniProt
brenda
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brenda
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metabolism
the enzyme is involved in the ethylmalonyl-CoA pathway, an acetyl-CoA assimilation strategy
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62300
2 * 62300, N-terminal histidine-tagged fusion protein, SDS-PAGE
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homodimer
2 * 62300, N-terminal histidine-tagged fusion protein, SDS-PAGE
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expression in Escherichia coli as a N-terminal histidine-tagged fusion protein
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Erb, T.J.; Fuchs, G.; Alber, B.E.
(2S)-Methylsuccinyl-CoA dehydrogenase closes the ethylmalonyl-CoA pathway for acetyl-CoA assimilation
Mol. Microbiol.
73
992-1008
2009
Luteovulum sphaeroides (D3JV03)
brenda
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