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Literature summary extracted from

  • Rojas, C.; Schmidt, J.; Lee, M.Y.; Gustafson, W.G.; McFarland, J.T.
    Structure-function correlation of fatty acyl-CoA dehydrogenase and fatty acyl-CoA oxidase (1985), Biochemistry, 24, 2947-2954.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.8.7 0.001
-
 beta(2-furyl)propionyl-CoA at pH 6.7 Sus scrofa
1.3.8.7 0.007
-
 beta(2-furyl)propionyl-CoA at pH 8.5 Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.7 Sus scrofa
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.8.7 a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein mechanism, proton abstraction from C-2 of the substrate and hydride transfer from C-3 to the N-5 position of the flavin Sus scrofa
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.8.7 liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.8.7 beta-(2-furyl)propionyl-CoA + electron transfer flavoprotein + 2,6-dichloroindophenol
-
 Sus scrofa trans-beta-(2-furyl)acryloyl-CoA + reduced acceptor
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.8.7 8
-
-
 Sus scrofa
1.3.8.7 8.5
-
-
 Sus scrofa

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.3.8.7 6.5 8.5 increasing activity with increasing pH Sus scrofa