Aldehyde oxidase 1

Aldehyde oxidase 1

Identifiers

AOX1 ; AO; AOH1

External IDs

OMIM: 602841 MGI: 88035 HomoloGene: 68165 ChEMBL: 3257 GeneCards: AOX1 Gene

Gene ontology
Molecular function	• aldehyde oxidase activity • xanthine dehydrogenase activity • iron ion binding • UDP-N-acetylmuramate dehydrogenase activity • electron carrier activity • molybdopterin cofactor binding • flavin adenine dinucleotide binding • NAD binding • 2 iron, 2 sulfur cluster binding
Cellular component	• cytoplasm
Biological process	• inflammatory response • reactive oxygen species metabolic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

ENSG00000138356

ENSMUSG00000063558

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
201.45 – 201.54 Mb

Chr 1:
58.03 – 58.11 Mb

PubMed search

Aldehyde oxidase 1 is an enzyme that in humans is encoded by the AOX1 gene.^[1]^[2]

Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide.^[1]

Clinical significance

Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis.^[2]

See also

MOCOS

References

↑ 1.0 1.1 "Entrez Gene: aldehyde oxidase 1".
↑ 2.0 2.1 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.

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.
Rose JE, Behm FM, Drgon T et al. "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, OrsÃ³ 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.
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. 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ross CJ, Katzov-Eckert H, DubÃ© 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.