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Literature summary for 1.3.3.6 extracted from

  • Ferdinandusse, S.; Denis, S.; van Roermund, C.W.T.; Preece, M.A.; Koster, J.; Ebberink, M.S.; Waterham, H.R.; Wanders, R.J.A.
    A novel case of ACOX2 deficiency leads to recognition of a third human peroxisomal acyl-CoA oxidase (2018), Biochim. Biophys. Acta Mol. Basis Dis., 1864, 952-958 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae Homo sapiens

Localization

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

Organism

Organism UniProt Comment Textmining
Homo sapiens O15254
-
-
Homo sapiens Q15067
-
-
Homo sapiens Q99424
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Homo sapiens
-
liver highest expression Homo sapiens
-
pancreas
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
decanoyl-CoA + O2
-
Homo sapiens trans-2,3-dehydrodecanoyl-CoA + H2O2
-
?
hexadecanoyl-CoA + O2
-
Homo sapiens trans-2,3-dehydrohexadecanoyl-CoA + H2O2
-
?
additional information isoform ACOX1 is responsible for the oxidation of straight-chain fatty acids with different chain lengths Homo sapiens ?
-
-
additional information isoform ACOX2 is the only human acyl-CoA oxidase involved in bile acid biosynthesis, and is involved in the degradation of the branched-chain fatty acids Homo sapiens ?
-
-
additional information isoform ACOX3 is involved in the degradation of the branched-chain fatty acids Homo sapiens ?
-
-
pristanoyl-CoA + O2
-
Homo sapiens trans-2,3-dehydropristanoyl-CoA + H2O2
-
?
trihydroxycholestanoyl-CoA + O2
-
Homo sapiens trans-2,3-dehydrotrihydroxycholestanoyl-CoA + H2O2
-
?

Subunits

Subunits Comment Organism
? x * 51000, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
ACOX1 isoform Homo sapiens
ACOX2 isoform Homo sapiens
ACOX3 isoform Homo sapiens

General Information

General Information Comment Organism
malfunction isoform ACOX2 deficiency leads to a Zellweger spectrum disorder lacking functional peroxisomes Homo sapiens