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AOX1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4UHW, 4UHX, 5EPG
Identifiers
Aliases	AOX1, AO, AOH1, aldehyde oxidase 1
External IDs	OMIM: 602841; MGI: 88035; HomoloGene: 68165; GeneCards: AOX1; OMA:AOX1 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q33.1 Start 200,586,014 bp End 200,677,064 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 C1.3|1 28.86 cM Start 58,069,090 bp End 58,145,572 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal cortex left adrenal cortex right lobe of liver body of pancreas left uterine tube germinal epithelium subcutaneous adipose tissue right ovary kidney tubule gastric mucosa Top expressed in left lobe of liver tunica adventitia of aorta lumbar spinal ganglion brown adipose tissue soleus muscle tunica media of zone of aorta white adipose tissue facial motor nucleus esophagus intercostal muscle More reference expression data BioGPS n/a
Gene ontology Molecular function oxidoreductase activity, acting on CH-OH group of donors iron-sulfur cluster binding NAD binding metal ion binding catalytic activity electron transfer activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors aldehyde oxidase activity iron ion binding protein homodimerization activity molybdopterin cofactor binding flavin adenine dinucleotide binding 2 iron, 2 sulfur cluster binding identical protein binding xanthine dehydrogenase activity FAD binding Cellular component extracellular exosome cytoplasm cytosol nuclear body Biological process xanthine catabolic process vitamin B6 metabolic process electron transport chain Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 316 11761 Ensembl ENSG00000138356 ENSMUSG00000063558 UniProt Q06278 O54754 RefSeq (mRNA) NM_001159 NM_009676 RefSeq (protein) NP_001150 NP_033806 Location (UCSC) Chr 2: 200.59 – 200.68 Mb Chr 1: 58.07 – 58.15 Mb PubMed search
Wikidata
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Aldehyde oxidase 1 is an enzyme that in humans is encoded by the AOX1 gene.

Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide.

Clinical significance

Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis.

See also

• MOCOS

References

1. ^ GRCh38: Ensembl release 89: ENSG00000138356 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000063558 – 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. ^ "Entrez Gene: aldehyde oxidase 1".
6. ^ Berger R, Mezey E, Clancy KP, Harta G, Wright RM, Repine JE, Brown RH, Brownstein M, Patterson D (March 1995). "Analysis of aldehyde oxidase and xanthine dehydrogenase/oxidase as possible candidate genes for autosomal recessive familial amyotrophic lateral sclerosis". Somat. Cell Mol. Genet. 21 (2): 121–31. doi:10.1007/BF02255787. PMID 7570184. S2CID 24691533.

External links

• Human AOX1 genome location and AOX1 gene details page in the UCSC Genome Browser.

Further reading

• Wang AG, Yoon SY, Oh JH, et al. (2006). "Identification of intrahepatic cholangiocarcinoma related genes by comparison with normal liver tissues using expressed sequence tags". Biochem. Biophys. Res. Commun. 345 (3): 1022–32. doi:10.1016/j.bbrc.2006.04.175. PMID 16712791.
• Smith MA, Marinaki AM, Arenas M, et al. (2009). "Novel pharmacogenetic markers for treatment outcome in azathioprine-treated inflammatory bowel disease". Aliment. Pharmacol. Ther. 30 (4): 375–84. doi:10.1111/j.1365-2036.2009.04057.x. PMID 19500084. S2CID 1292701.
• Rose JE, Behm FM, Drgon T, et al. (2010). "Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score". Mol. Med. 16 (7–8): 247–53. doi:10.2119/molmed.2009.00159. PMC 2896464. PMID 20379614.
• Sigruener A, Buechler C, Orsó E, et al. (2007). "Human aldehyde oxidase 1 interacts with ATP-binding cassette transporter-1 and modulates its activity in hepatocytes". Horm. Metab. Res. 39 (11): 781–9. doi:10.1055/s-2007-992129. PMID 17992631. S2CID 28460089.
• Ichida K, Matsumura T, Sakuma R, et al. (2001). "Mutation of human molybdenum cofactor sulfurase gene is responsible for classical xanthinuria type II". Biochem. Biophys. Res. Commun. 282 (5): 1194–200. doi:10.1006/bbrc.2001.4719. PMID 11302742.
• Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Alfaro JF, Joswig-Jones CA, Ouyang W, et al. (2009). "Purification and mechanism of human aldehyde oxidase expressed in Escherichia coli". Drug Metab. Dispos. 37 (12): 2393–8. doi:10.1124/dmd.109.029520. PMC 2784701. PMID 19741035.
• Rodrigues AD (1994). "Comparison of levels of aldehyde oxidase with cytochrome P450 activities in human liver in vitro". Biochem. Pharmacol. 48 (1): 197–200. doi:10.1016/0006-2952(94)90240-2. PMID 8043023.
• Wright RM, Vaitaitis GM, Wilson CM, et al. (1993). "cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase". Proc. Natl. Acad. Sci. U.S.A. 90 (22): 10690–4. Bibcode:1993PNAS...9010690W. doi:10.1073/pnas.90.22.10690. PMC 47843. PMID 8248161.
• Buechler C, Boettcher A, Bared SM, et al. (2002). "The carboxyterminus of the ATP-binding cassette transporter A1 interacts with a beta2-syntrophin/utrophin complex". Biochem. Biophys. Res. Commun. 293 (2): 759–65. doi:10.1016/S0006-291X(02)00303-0. PMID 12054535.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
• Ross CJ, Katzov-Eckert H, Dubé MP, et al. (2009). "Genetic variants in TPMT and COMT are associated with hearing loss in children receiving cisplatin chemotherapy". Nat. Genet. 41 (12): 1345–9. doi:10.1038/ng.478. PMID 19898482. S2CID 21293339.

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