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{{Infobox_gene}}
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'''Peroxisomal acyl-coenzyme A oxidase 1''' is an [[enzyme]] that in humans is encoded by the ''ACOX1'' [[gene]].<ref name="pmid8159712">{{cite journal | vauthors = Varanasi U, Chu R, Chu S, Espinosa R, LeBeau MM, Reddy JK | title = Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization | journal = Proc Natl Acad Sci U S A | volume = 91 | issue = 8 | pages = 3107–11 |date=May 1994 | pmid = 8159712 | pmc = 43524 | doi =10.1073/pnas.91.8.3107 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Acyl-Coenzyme A oxidase 1, palmitoyl
| HGNCid = 119
| Symbol = ACOX1
| AltSymbols =; ACOX; MGC1198; PALMCOX; SCOX
| OMIM = 609751
| ECnumber = 
| Homologene = 38299
| MGIid = 1330812
| GeneAtlas_image1 = PBB_GE_ACOX1_209600_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ACOX1_213501_at_tn.png
| Function = {{GNF_GO|id=GO:0003995 |text = acyl-CoA dehydrogenase activity}} {{GNF_GO|id=GO:0003997 |text = acyl-CoA oxidase activity}} {{GNF_GO|id=GO:0009053 |text = electron donor activity}} {{GNF_GO|id=GO:0050660 |text = FAD binding}}
| Component = {{GNF_GO|id=GO:0005777 |text = peroxisome}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006635 |text = fatty acid beta-oxidation}} {{GNF_GO|id=GO:0006693 |text = prostaglandin metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51
    | Hs_Ensembl = ENSG00000161533
    | Hs_RefseqProtein = NP_004026
    | Hs_RefseqmRNA = NM_004035
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 71453260
    | Hs_GenLoc_end = 71487039
    | Hs_Uniprot = Q15067
    | Mm_EntrezGene = 11430
    | Mm_Ensembl = ENSMUSG00000020777
    | Mm_RefseqmRNA = NM_015729
    | Mm_RefseqProtein = NP_056544
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 115987978
    | Mm_GenLoc_end = 116015135
    | Mm_Uniprot = Q9R0H0
  }}
}}
'''Acyl-Coenzyme A oxidase 1, palmitoyl''', also known as '''ACOX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =
| summary_text = 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 acid]]s. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}
==See also==
* [[ACOX3]]
* [[Acyl-CoA oxidase]]


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ACOX1}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Seedorf U, Ellinghaus P, Roch Nofer J |title=Sterol carrier protein-2. |journal=Biochim. Biophys. Acta |volume=1486 |issue= 1 |pages= 45-54 |year= 2000 |pmid= 10856712 |doi=  }}
*{{cite journal  | vauthors=Seedorf U, Ellinghaus P, Roch Nofer J |title=Sterol carrier protein-2. |journal=Biochim. Biophys. Acta |volume=1486 |issue= 1 |pages= 45–54 |year= 2000 |pmid= 10856712 |doi=  10.1016/s1388-1981(00)00047-0}}
*{{cite journal  | author=Singh H, Brogan M, Johnson D, Poulos A |title=Peroxisomal beta-oxidation of branched chain fatty acids in human skin fibroblasts. |journal=J. Lipid Res. |volume=33 |issue= 11 |pages= 1597-605 |year= 1993 |pmid= 1464743 |doi=  }}
*{{cite journal  | vauthors=Singh H, Brogan M, Johnson D, Poulos A |title=Peroxisomal beta-oxidation of branched chain fatty acids in human skin fibroblasts. |journal=J. Lipid Res. |volume=33 |issue= 11 |pages= 1597–605 |year= 1993 |pmid= 1464743 |doi=  }}
*{{cite journal  | author=Watkins PA, McGuinness MC, Raymond GV, ''et al.'' |title=Distinction between peroxisomal bifunctional enzyme and acyl-CoA oxidase deficiencies. |journal=Ann. Neurol. |volume=38 |issue= 3 |pages= 472-7 |year= 1995 |pmid= 7668838 |doi= 10.1002/ana.410380322 }}
*{{cite journal  | vauthors=Watkins PA, McGuinness MC, Raymond GV |title=Distinction between peroxisomal bifunctional enzyme and acyl-CoA oxidase deficiencies. |journal=Ann. Neurol. |volume=38 |issue= 3 |pages= 472–7 |year= 1995 |pmid= 7668838 |doi= 10.1002/ana.410380322 |display-authors=etal}}
*{{cite journal  | author=Chu R, Varanasi U, Chu S, ''et al.'' |title=Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4908-15 |year= 1995 |pmid= 7876265 |doi=  }}
*{{cite journal  | vauthors=Chu R, Varanasi U, Chu S |title=Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4908–15 |year= 1995 |pmid= 7876265 |doi=10.1074/jbc.270.9.4908 |display-authors=etal}}
*{{cite journal  | author=Fournier B, Saudubray JM, Benichou B, ''et al.'' |title=Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 526-31 |year= 1994 |pmid= 8040306 |doi=  }}
*{{cite journal  | vauthors=Fournier B, Saudubray JM, Benichou B |title=Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 526–31 |year= 1994 |pmid= 8040306 |doi=10.1172/JCI117365 | pmc=296126  |display-authors=etal}}
*{{cite journal  | author=Aoyama T, Tsushima K, Souri M, ''et al.'' |title=Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. |journal=Biochem. Biophys. Res. Commun. |volume=198 |issue= 3 |pages= 1113-8 |year= 1994 |pmid= 8117268 |doi= 10.1006/bbrc.1994.1158 }}
*{{cite journal  | vauthors=Aoyama T, Tsushima K, Souri M |title=Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase. |journal=Biochem. Biophys. Res. Commun. |volume=198 |issue= 3 |pages= 1113–8 |year= 1994 |pmid= 8117268 |doi= 10.1006/bbrc.1994.1158 |display-authors=etal}}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal  | author=Varanasi U, Chu R, Chu S, ''et al.'' |title=Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 3107-11 |year= 1994 |pmid= 8159712 |doi=  }}
*{{cite journal  | vauthors=Pacot C, Latruffe N |title=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 |journal=Biochimie |volume=75 |issue= 3–4 |pages= 235–42 |year= 1993 |pmid= 8507686 |doi=10.1016/0300-9084(93)90082-4 }}
*{{cite journal  | author=Pacot C, Latruffe N |title=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. |journal=Biochimie |volume=75 |issue= 3-4 |pages= 235-42 |year= 1993 |pmid= 8507686 |doi=  }}
*{{cite journal  | vauthors=Fan CY, Pan J, Chu R |title=Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase gene |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24698–710 |year= 1996 |pmid= 8798738 |doi=10.1074/jbc.271.40.24698 |display-authors=etal}}
*{{cite journal  | author=Fan CY, Pan J, Chu R, ''et al.'' |title=Hepatocellular and hepatic peroxisomal alterations in mice with a disrupted peroxisomal fatty acyl-coenzyme A oxidase gene. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24698-710 |year= 1996 |pmid= 8798738 |doi=  }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal  | vauthors=Fujiwara C, Imamura A, Hashiguchi N |title=Catalase-less peroxisomes. Implication in the milder forms of peroxisome biogenesis disorder |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 37271–7 |year= 2001 |pmid= 10960480 |doi= 10.1074/jbc.M006347200 |display-authors=etal}}
*{{cite journal  | author=Fujiwara C, Imamura A, Hashiguchi N, ''et al.'' |title=Catalase-less peroxisomes. Implication in the milder forms of peroxisome biogenesis disorder. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 37271-7 |year= 2001 |pmid= 10960480 |doi= 10.1074/jbc.M006347200 }}
*{{cite journal  | vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948  }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | vauthors=Wiemann S, Weil B, Wellenreuther R |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R | pmc=311072 |display-authors=etal}}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | vauthors=Suzuki Y, Iai M, Kamei A |title=Peroxisomal acyl CoA oxidase deficiency |journal=J. Pediatr. |volume=140 |issue= 1 |pages= 128–30 |year= 2002 |pmid= 11815777 |doi=10.1067/mpd.2002.120511  |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Iai M, Kamei A, ''et al.'' |title=Peroxisomal acyl CoA oxidase deficiency. |journal=J. Pediatr. |volume=140 |issue= 1 |pages= 128-30 |year= 2002 |pmid= 11815777 |doi= }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | vauthors=Wiemann S, Arlt D, Huber W |title=From ORFeome to biology: a functional genomics pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 |display-authors=etal}}
*{{cite journal | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
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[[Category:Human proteins]]
 
 
{{gene-17-stub}}

Latest revision as of 17:44, 29 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Peroxisomal acyl-coenzyme A oxidase 1 is an enzyme that in humans is encoded by the ACOX1 gene.[1][2]

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.[2]

See also

References

  1. ↑ 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. doi:10.1073/pnas.91.8.3107. PMC 43524. PMID 8159712.
  2. ↑ 2.0 2.1 "Entrez Gene: ACOX1 acyl-Coenzyme A oxidase 1, palmitoyl".

External links

Further reading


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