Aldehyde oxidase 1

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	Wikidata
View/Edit Human

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[edit | edit source]

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

References[edit | edit source]

↑ ^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.

External links[edit | edit source]

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

Further reading[edit | edit source]

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; 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.
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, 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.

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[entrez-1] 1.0 ^1.1 "Entrez Gene: aldehyde oxidase 1".

[pmid7570184-2] 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.

[1]

[2]

v t e Aldehyde/oxo oxidoreductases (EC 1.2)
1.2.1: NAD or NADP	Aldehyde dehydrogenase Acetaldehyde dehydrogenase Long-chain-aldehyde dehydrogenase
1.2.2: cytochrome	Formate dehydrogenase (cytochrome)
1.2.3: oxygen	Aldehyde oxidase
1.2.4: disulfide	Oxoglutarate dehydrogenase complex Pyruvate dehydrogenase Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD
1.2.7: iron-sulfur protein	Pyruvate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

Aldehyde oxidase 1

Contents

Clinical significance[edit | edit source]

See also[edit | edit source]

References[edit | edit source]

External links[edit | edit source]

Further reading[edit | edit source]