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Literature summary for 1.3.8.7 extracted from

  • Lau, S.M.; Brantley, R.K.; Thorpe, C.
    The reductive half-reaction in Acyl-CoA dehydrogenase from pig kidney: studies with thiaoctanoyl-CoA and oxaoctanoyl-CoA analogues (1988), Biochemistry, 27, 5089-5095.
    View publication on PubMed
Search for more literature for 1.3.8.7

Cloned(Commentary)

Cloned (Comment) Organism
-
 Sus scrofa

Inhibitors

Inhibitors Comment Organism Structure
3-oxaoctanoyl-CoA
-
 Sus scrofa
3-thiaoctanoyl-CoA
-
 Sus scrofa
4-oxaoctanoyl-CoA
-
 Sus scrofa
4-thiaoctanoyl-CoA
-
 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
kidney
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-oxaoctanoyl-CoA + phenazine methosulfate + 2,6-dichlorophenolindophenol poor substrate, oxidized at about 10% of the rate of octanoyl-CoA Sus scrofa 4-thia-trans-2-octenoyl-CoA + reduced 2,6-dichlorophenolindophenol
-
 ?
4-thiaoctanoyl-CoA + phenazine methosulfate + 2,6-dichlorophenolindophenol oxidized 1.5fold faster than octanoyl-CoA Sus scrofa 4-thia-trans-2-octenoyl-CoA + reduced 2,6-dichlorophenolindophenol
-
 ?