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Literature summary for 1.3.8.1 extracted from

  • Kean, E.A.
    Selective inhibition of acyl-CoA dehydrogenases by a metabolite of hypoglycin (1976), Biochim. Biophys. Acta, 422, 8-14.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
(methylenecyclopropyl)acetyl-CoA 0.0129 mM and 0.0172 mM, strong inhibition of enzyme activity in enzyme mixture Oryctolagus cuniculus
(methylenecyclopropyl)acetyl-CoA
-
Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0024
-
butyryl-CoA partially purified enzyme, enzyme mixture Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Rattus norvegicus 5739
-

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.48
-
partially purified enzyme mixture, substrate butyryl-CoA Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyryl-CoA + 2,6-dichloro-phenolindophenol
-
Oryctolagus cuniculus but-2-enoyl-CoA + reduced 2,6-dichloro-phenolindophenol
-
r