Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.8.1 0.0024
-
butyryl-CoA partially purified enzyme, enzyme mixture Oryctolagus cuniculus

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
1.3.8.1 Oryctolagus cuniculus
-
-
-
1.3.8.1 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.8.1 liver
-
Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.8.1 0.48
-
partially purified enzyme mixture, substrate butyryl-CoA Oryctolagus cuniculus

Substrates and Products (Substrate)

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