Aldehyde oxidase 1

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
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	200,677,064 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	58,106,413 bp[2]
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; • geranial:oxygen oxidoreductase activity; • heptaldehyde:oxygen oxidoreductase activity; • 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; • drug metabolic process; • oxidation-reduction process; • electron transport chain;
	Sources:Amigo / QuickGO
Orthologs
	316
	11761
	ENSG00000138356
	ENSMUSG00000063558
	Q06278
	O54754
	NM_001159
	NM_009676
	NP_001150
	NP_033806
	Wikidata
View/Edit Human	View/Edit Mouse

Aldehyde oxidase 1 is an enzyme that in humans is encoded by the AOX1 gene.[5][6]

Aldehyde oxidase produces hydrogen peroxide and, under certain conditions, can catalyze the formation of superoxide.[5]

Clinical significance

Aldehyde oxidase is a candidate gene for amyotrophic lateral sclerosis.[6]

References

GRCh38: Ensembl release 89: ENSG00000138356 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000063558 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: aldehyde oxidase 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" (PDF). Somat. Cell Mol. Genet. 21 (2): 121–31. doi:10.1007/BF02255787. PMID 7570184.

External links

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

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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000138356 - Ensembl, May 2017

[refGRCm38Ensembl-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.

[entrez-5] "Entrez Gene: aldehyde oxidase 1".

[pmid7570184-6] 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" (PDF). Somat. Cell Mol. Genet. 21 (2): 121–31. doi:10.1007/BF02255787. PMID 7570184.

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

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) EC7 Translocases (list)

Aldehyde oxidase 1

Clinical significance

See also

References

External links

Further reading