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Gene Review

ACOX2  -  acyl-CoA oxidase 2, branched chain

Homo sapiens

Synonyms: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase, 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase, BCOX, BRCACOX, BRCOX, ...
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High impact information on ACOX2

  • Possible candidate genes in this region include GBE1 and ACOX2, which encode enzymes involved in glycogen and fatty acid metabolism, respectively [1].
  • The obtained sequence showed 73.6% similarity with a proposed rat THCA-CoA oxidase and 81% similarity with a recently reported human branched chain acyl-CoA oxidase, indicating that these three proteins represent the same enzyme [2].
  • We here describe the cloning and sequencing of a cDNA coding the first of these enzymes, a 3alpha,7alpha,12alpha-trihydroxy-5beta-choles tanoyl-CoA oxidase (THCA-CoA oxidase) from rabbit liver peroxisomes [2].
  • Transfection of COS cells with the coding part of the cDNA resulted in a significant expression of THCA-CoA oxidase activity [2].
  • The column eluates were assayed for palmitoyl-CoA and trihydroxycoprostanoyl-CoA oxidase activities and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis [3].

Biological context of ACOX2


Anatomical context of ACOX2

  • We conclude that these two cell lines have defects in two enzyme activities involved in the peroxisomal oxidation in bile acid formation, the microsomal THCA-CoA ligase and the peroxisomal THCA-CoA oxidase [5].

Associations of ACOX2 with chemical compounds


Other interactions of ACOX2


  1. Linkage of serum insulin concentrations to chromosome 3p in Mexican Americans. Mitchell, B.D., Cole, S.A., Hsueh, W.C., Comuzzie, A.G., Blangero, J., MacCluer, J.W., Hixson, J.E. Diabetes (2000) [Pubmed]
  2. Molecular cloning and expression of cDNA encoding 3alpha,7alpha,12alpha-trihydroxy-5beta-chole stanoyl-CoA oxidase from rabbit liver. Pedersen, J.I., Eggertsen, G., Hellman, U., Andersson, U., Björkhem, I. J. Biol. Chem. (1997) [Pubmed]
  3. Presence of three acyl-CoA oxidases in rat liver peroxisomes. An inducible fatty acyl-CoA oxidase, a noninducible fatty acyl-CoA oxidase, and a noninducible trihydroxycoprostanoyl-CoA oxidase. Schepers, L., Van Veldhoven, P.P., Casteels, M., Eyssen, H.J., Mannaerts, G.P. J. Biol. Chem. (1990) [Pubmed]
  4. Evidence for the existence of a pristanoyl-CoA oxidase gene in man. Vanhooren, J.C., Marynen, P., Mannaerts, G.P., Van Veldhoven, P.P. Biochem. J. (1997) [Pubmed]
  5. Human hepatoblastoma cells (HepG2) and rat hepatoma cells are defective in important enzyme activities in the oxidation of the C27 steroid side chain in bile acid formation. Farrants, A.K., Nilsson, A., Pedersen, J.I. J. Lipid Res. (1993) [Pubmed]
  6. Peroxisomal lipid degradation via beta- and alpha-oxidation in mammals. Mannaerts, G.P., Van Veldhoven, P.P., Casteels, M. Cell Biochem. Biophys. (2000) [Pubmed]
  7. Separate peroxisomal oxidases for fatty acyl-CoAs and trihydroxycoprostanoyl-CoA in human liver. Casteels, M., Schepers, L., Van Veldhoven, P.P., Eyssen, H.J., Mannaerts, G.P. J. Lipid Res. (1990) [Pubmed]
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