Literature summary for 1.3.8.7 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.

Search for more literature for 1.3.8.7

KM Value [mM]

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

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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

Source Tissue	Comment	Organism	Textmining
liver	-	Sus scrofa	-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	-	Sus scrofa
8.5	-	-	Sus scrofa

pH Range

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)