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

BRENDA support

Literature summary extracted from

  • Bronfman, M.; Inestrosa, N.C.; Nervi, F.O.; Leighton, F.
    Acyl-CoA synthetase and the peroxisomal enzymes of beta-oxidation in human liver. Quantitative analysis of their subcellular localization (1984), Biochem. J., 224, 709-720.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.3.6 peroxisome
-
 Homo sapiens 5777
-

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 Homo sapiens 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 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.6 partially Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.3.6 liver
-
 Homo sapiens
-

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 additional information
-
-
 Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Homo sapiens trans-2,3-dehydroacyl-CoA + H2O2
-
 ?
1.3.3.6 palmitoyl-CoA + O2
-
 Homo sapiens 2-trans-hexadecenoyl-CoA + H2O2
-
 ?