ACOX1

ACOX1
Identifiers
Aliases	ACOX1 , ACOX, PALMCOX, SCOX, acyl-CoA oxidase 1, palmitoyl, acyl-CoA oxidase 1, MITCH
External IDs	OMIM: 609751 MGI: 1330812 HomoloGene: 38299 GeneCards: ACOX1
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17q25.1 Start 75,941,507 bp [1] End 75,979,177 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11|11 E2 Start 116,062,714 bp [2] End 116,089,871 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa duodenum liver right lobe of liver internal globus pallidus cavity of mouth rectum blood islet of Langerhans body of pancreas Top expressed in left lobe of liver proximal tubule kidney brown adipose tissue pyloric antrum epithelium of stomach jejunum white adipose tissue mucous cell of stomach pineal gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function signaling receptor binding PDZ domain binding palmitoyl-CoA oxidase activity protein N-terminus binding oxidoreductase activity oxidoreductase activity, acting on the CH-CH group of donors acyl-CoA oxidase activity FAD binding acyl-CoA dehydrogenase activity flavin adenine dinucleotide binding fatty acid binding Cellular component nucleolus nucleoplasm cytoplasm mitochondrion nucleus peroxisomal membrane intracellular membrane-bounded organelle peroxisome membrane peroxisomal matrix plasma membrane cytosol Biological process spermatogenesis generation of precursor metabolites and energy lipid metabolism fatty acid beta-oxidation alpha-linolenic acid metabolic process metabolism peroxisome fission fatty acid metabolic process very long-chain fatty acid metabolic process prostaglandin metabolic process lipid homeostasis fatty acid oxidation fatty acid beta-oxidation using acyl-CoA oxidase regulation of lipid metabolic process fatty acid beta-oxidation using acyl-CoA dehydrogenase protein targeting to peroxisome Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51 11430 Ensembl ENSG00000161533 ENSMUSG00000020777 UniProt Q15067 Q9R0H0 RefSeq (mRNA) NM_001185039 NM_004035 NM_007292 NM_001271898 NM_015729 NM_001377521 NM_001377522 RefSeq (protein) NP_001171968 NP_004026 NP_009223 NP_001258827 NP_056544 NP_001364450 NP_001364451 Location (UCSC) Chr 17: 75.94 – 75.98 Mb Chr 11: 116.06 – 116.09 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Peroxisomal acyl-coenzyme A oxidase 1 is an enzyme that in humans is encoded by the ACOX1 gene. ^{[5] [6]}

The protein encoded by this gene is the first enzyme of the fatty acid beta-oxidation pathway, which catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. It donates electrons directly to molecular oxygen, thereby producing hydrogen peroxide. Defects in this gene result in pseudoneonatal adrenoleukodystrophy, a disease that is characterized by accumulation of very long chain fatty acids. Alternatively spliced transcript variants encoding different isoforms have been identified. ^[6]

See also

• ACOX3
• Acyl-CoA oxidase

References

1. GRCh38: Ensembl release 89: ENSG00000161533 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020777 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK (May 1994). "Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization". Proc Natl Acad Sci U S A. 91 (8): 3107–11. Bibcode:1994PNAS...91.3107V. doi: 10.1073/pnas.91.8.3107 . PMC   43524 . PMID   8159712.
6. "Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl".

External links

• Human ACOX1 genome location and ACOX1 gene details page in the UCSC Genome Browser .

Further reading

• Seedorf U, Ellinghaus P, Roch Nofer J (2000). "Sterol carrier protein-2". Biochim. Biophys. Acta. 1486 (1): 45–54. doi:10.1016/s1388-1981(00)00047-0. PMID   10856712.
• Singh H, Brogan M, Johnson D, Poulos A (1993). "Peroxisomal beta-oxidation of branched chain fatty acids in human skin fibroblasts". J. Lipid Res. 33 (11): 1597–605. doi: 10.1016/S0022-2275(20)41382-3 . PMID   1464743.
• Watkins PA, McGuinness MC, Raymond GV, et al. (1995). "Distinction between peroxisomal bifunctional enzyme and acyl-CoA oxidase deficiencies". Ann. Neurol. 38 (3): 472–7. doi:10.1002/ana.410380322. PMID   7668838. S2CID   8189860.
• Chu R, Varanasi U, Chu S, et al. (1995). "Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells". J. Biol. Chem. 270 (9): 4908–15. doi: 10.1074/jbc.270.9.4908 . PMID   7876265.
• Fournier B, Saudubray JM, Benichou B, et al. (1994). "Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy". J. Clin. Invest. 94 (2): 526–31. doi:10.1172/JCI117365. PMC   296126 . PMID   8040306.
• Aoyama T, Tsushima K, Souri M, et al. (1994). "Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase". Biochem. Biophys. Res. Commun. 198 (3): 1113–8. doi:10.1006/bbrc.1994.1158. PMID   8117268.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Pacot C, Latruffe N (1993). "Biochemical properties of liver peroxisomes from rat, guinea pig and human species and the influence of hormonal status on rat liver acyl-CoA oxidase mRNA content". Biochimie. 75 (3–4): 235–42. doi:10.1016/0300-9084(93)90082-4. PMID   8507686.
• Fan CY, Pan J, Chu R, et al. (1996). "Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase gene". J. Biol. Chem. 271 (40): 24698–710. doi: 10.1074/jbc.271.40.24698 . PMID   8798738.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Fujiwara C, Imamura A, Hashiguchi N, et al. (2001). "Catalase-less peroxisomes. Implication in the milder forms of peroxisome biogenesis disorder". J. Biol. Chem. 275 (47): 37271–7. doi: 10.1074/jbc.M006347200 . PMID   10960480.
• Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC   310948 . PMID   11076863.
• Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC   311072 . PMID   11230166.
• Suzuki Y, Iai M, Kamei A, et al. (2002). "Peroxisomal acyl CoA oxidase deficiency". J. Pediatr. 140 (1): 128–30. doi:10.1067/mpd.2002.120511. PMID   11815777. S2CID   36469133.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC   528930 . PMID   15489336.