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Literature summary extracted from

  • Inestrosa, N.C.; Bronfman, M.; Leighton, F.
    Purification of the peroxisomal fatty acyl-CoA oxidase from rat liver (1980), Biochem. Biophys. Res. Commun., 95, 7-12.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.3.3.6 stabilization with benzoate necessary for purification of the holoenzyme Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.3.6 peroxisome
-
 Rattus norvegicus 5777
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.3.6 22000
-
 2 * 45000 + 2 * 22000, SDS-PAGE Rattus norvegicus
1.3.3.6 45000
-
 2 * 45000 + 2 * 22000, SDS-PAGE Rattus norvegicus
1.3.3.6 136000
-
 gel filtration Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.6 acyl-CoA + O2 Rattus norvegicus CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process trans-2,3-dehydroacyl-CoA + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.6 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.6 holo- and apoenzyme Rattus norvegicus

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.3.6 27.2
-
 purified enzyme Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.6 acyl-CoA + O2
-
 Rattus norvegicus trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 acyl-CoA + O2 CoA derivatives of fatty acids with chain length from 8 to 18, first reaction of peroxisomal beta-oxidation, rate limiting for this process Rattus norvegicus trans-2,3-dehydroacyl-CoA + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.3.6 tetramer 2 * 45000 + 2 * 22000, SDS-PAGE Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.3.6 FAD flavoprotein with noncovalently bound FAD Rattus norvegicus