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ACOX3  -  acyl-CoA oxidase 3, pristanoyl

Homo sapiens

Synonyms: BRCACox, BRCOX, Branched-chain acyl-CoA oxidase, PRCOX, Peroxisomal acyl-coenzyme A oxidase 3, ...
 
 
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Disease relevance of ACOX3

  • Furthermore, our data suggest that pristanoyl-CoA oxidase (ACOX3), which is expressed at extremely low level in other human organs studied including the liver, might contribute significantly to peroxisomal branched chain fatty acid beta-oxidation in human prostate tissue and some prostate cancer cell lines [1].
 

High impact information on ACOX3

  • Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome [2].
  • Peroxisomes in human liver contain two distinct acyl-CoA oxidases with different substrate specificities: (i) palmitoyl-CoA oxidase, oxidizing very long straight-chain fatty acids and eicosanoids, and (ii) a branched-chain acyl-CoA oxidase (hBRCACox), involved in the degradation of long branched fatty acids and bile acid intermediates [2].
  • Northern blot analysis demonstrated that--in contrast to the rTHCCox gene--the hBRCACox gene is transcribed also in extrahepatic tissues such as heart, kidney, skeletal muscle, and pancreas [2].
  • The composite cDNA sequence of hBRCACox, derived from overlapping clones isolated via immunoscreening and hybridization of human liver cDNA expression libraries, consisted of 2225 bases and contained an open reading frame of 2046 bases, encoding a protein of 681 amino acids with a calculated molecular mass of 76,739 Da [2].
  • 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 [3].
 

Biological context of ACOX3

 

Anatomical context of ACOX3

 

Associations of ACOX3 with chemical compounds

  • The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney [8].
  • These data, combined with the fact that the branched chain acyl-CoA oxidase, catalyzing the first oxidation step of pristanic acid and bile acid intermediates in man, appeared normal, suggested a peroxisomal beta-oxidation defect in the patient at the level of 2-methylacyl-CoA racemase [9].
 

Other interactions of ACOX3

  • 2-Methyl-branched acyl-CoAs are degraded via pristanoyl-CoA oxidase, multifunctional protein-2 (MFP-2) (which displays 2-enoyl-CoA hydratase and D-3-hydroxyacyl-CoA dehydrogenase activities) and sterol carrier protein-X (SCPX; displaying 2-methyl-3-oxoacyl-CoA thiolase activity) [10].
 

Analytical, diagnostic and therapeutic context of ACOX3

References

  1. Peroxisomal branched chain fatty acid beta-oxidation pathway is upregulated in prostate cancer. Zha, S., Ferdinandusse, S., Hicks, J.L., Denis, S., Dunn, T.A., Wanders, R.J., Luo, J., De Marzo, A.M., Isaacs, W.B. Prostate (2005) [Pubmed]
  2. Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome. Baumgart, E., Vanhooren, J.C., Fransen, M., Marynen, P., Puype, M., Vandekerckhove, J., Leunissen, J.A., Fahimi, H.D., Mannaerts, G.P., van Veldhoven, P.P. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  3. 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]
  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. Identification of pristanoyl-CoA oxidase and phytanic acid decarboxylation in peroxisomes and mitochondria from human liver: implications for Zellweger syndrome. Wanders, R.J., van Roermund, C.W., Jakobs, C., ten Brink, H.J. J. Inherit. Metab. Dis. (1991) [Pubmed]
  6. Assignment of the human peroxisomal branched-chain acyl-CoA oxidase gene to chromosome 3p21.1-p14.2 by rodent/human somatic cell hybridization. Moghrabi, N.N., Naylor, S.L., Van Veldhoven, P.P., Baumgart, E., Dawson, D.B., Bennett, M.J. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  7. Ataxia associated with increased plasma concentrations of pristanic acid, phytanic acid and C27 bile acids but normal fibroblast branched-chain fatty acid oxidation. Clayton, P.T., Johnson, A.W., Mills, K.A., Lynes, G.W., Wilson, J., Casteels, M., Mannaerts, G. J. Inherit. Metab. Dis. (1996) [Pubmed]
  8. The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney. Vanhove, G.F., Van Veldhoven, P.P., Fransen, M., Denis, S., Eyssen, H.J., Wanders, R.J., Mannaerts, G.P. J. Biol. Chem. (1993) [Pubmed]
  9. Fibroblast studies documenting a case of peroxisomal 2-methylacyl-CoA racemase deficiency: possible link between racemase deficiency and malabsorption and vitamin K deficiency. Van Veldhoven, P.P., Meyhi, E., Squires, R.H., Fransen, M., Fournier, B., Brys, V., Bennett, M.J., Mannaerts, G.P. Eur. J. Clin. Invest. (2001) [Pubmed]
  10. Peroxisomal lipid degradation via beta- and alpha-oxidation in mammals. Mannaerts, G.P., Van Veldhoven, P.P., Casteels, M. Cell Biochem. Biophys. (2000) [Pubmed]
  11. Maturation of peroxisomes in differentiating human hepatoblastoma cells (HepG2): possible involvement of the peroxisome proliferator-activated receptor alpha (PPAR alpha). Stier, H., Fahimi, H.D., Van Veldhoven, P.P., Mannaerts, G.P., Völkl, A., Baumgart, E. Differentiation (1998) [Pubmed]
 
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