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Q06278

- AOXA_HUMAN

UniProt

Q06278 - AOXA_HUMAN

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Protein

Aldehyde oxidase

Gene
AOX1, AO
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide and N-methylphthalazinium, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the reduction of nitrite to NO with NADH or aldehyde as electron donor. May play a role in adipogenesis.8 Publications

Catalytic activityi

An aldehyde + H2O + O2 = a carboxylate + H2O2.2 Publications
Retinal + O2 + H2O = retinoate + H2O2.2 Publications

Cofactori

Binds 2 2Fe-2S clusters per subunit.1 Publication
Binds 1 FAD per subunit.1 Publication
Binds 1 molybdenum-molybdopterin (Mo-MPT) cofactor per subunit.1 Publication

Enzyme regulationi

Is very potently inhibited by raloxifene. Also inhibited by estradiol, ethinyl estradiol, hydralazine, menadione, and isovanillin. Not inhibited by allopurinol, a xanthine dehydrogenase potent inhibitor.4 Publications

Kineticsi

kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and 5.6 min(-1) for chloroquinazolinone oxidation.

  1. KM=7.1 µM for benzaldehyde (at 25 degrees Celsius and pH 7.5)3 Publications
  2. KM=1.3 µM for phthalazine (at 25 degrees Celsius and pH 7.5)
  3. KM=3.9 µM for phenanthridine (at 25 degrees Celsius and pH 7.5)
  4. KM=5.2 µM for chloroquinazolinone (at 25 degrees Celsius and pH 7.5)
  5. KM=0.42 mM for 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)
  6. KM=0.15 mM for famciclovir (at 37 degrees Celsius and pH 7)
  7. KM=6.3 µM for N-[(2-dimethylamino)ethyl]acridine-4-carboxamide (at 37 degrees Celsius and pH 7.4)

Vmax=16 nmol/min/mg enzyme with 6-deoxypenciclovir as substrate

Vmax=61 nmol/min/mg enzyme with famciclovir as substrate

Vmax=2.3 nmol/min/mg enzyme with N-[(2-dimethylamino)ethyl]acridine-4-carboxamide as substrate

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi49 – 491Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi52 – 521Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi74 – 741Iron-sulfur 1 (2Fe-2S) By similarity
Binding sitei113 – 1131Molybdopterin By similarity
Metal bindingi114 – 1141Iron-sulfur 2 (2Fe-2S) By similarity
Metal bindingi117 – 1171Iron-sulfur 2 (2Fe-2S) By similarity
Metal bindingi149 – 1491Iron-sulfur 2 (2Fe-2S) By similarity
Metal bindingi151 – 1511Iron-sulfur 2 (2Fe-2S) By similarity
Binding sitei354 – 3541FAD By similarity
Binding sitei358 – 3581FAD By similarity
Binding sitei367 – 3671FAD By similarity
Binding sitei411 – 4111FAD; via amide nitrogen By similarity
Binding sitei806 – 8061Molybdopterin; via amide nitrogen By similarity
Binding sitei1047 – 10471Molybdopterin; via amide nitrogen By similarity
Binding sitei1203 – 12031Molybdopterin By similarity
Active sitei1270 – 12701Proton acceptor; for azaheterocycle hydroxylase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 2718FAD By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. aldehyde oxidase activity Source: Reactome
  3. electron carrier activity Source: InterPro
  4. flavin adenine dinucleotide binding Source: InterPro
  5. iron ion binding Source: InterPro
  6. molybdopterin cofactor binding Source: InterPro
  7. NAD binding Source: InterPro
  8. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  9. xanthine dehydrogenase activity Source: ProtInc

GO - Biological processi

  1. inflammatory response Source: ProtInc
  2. reactive oxygen species metabolic process Source: ProtInc
  3. small molecule metabolic process Source: Reactome
  4. vitamin B6 metabolic process Source: Reactome
  5. vitamin metabolic process Source: Reactome
  6. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138356-MONOMER.
ReactomeiREACT_25012. Vitamins B6 activation to pyridoxal phosphate.
SABIO-RKQ06278.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde oxidase (EC:1.2.3.1)
Alternative name(s):
Aldehyde oxidase 1
Azaheterocycle hydroxylase (EC:1.17.3.-)
Gene namesi
Name:AOX1
Synonyms:AO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:553. AOX1.

Subcellular locationi

Cytoplasm 3 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24842.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13381338Aldehyde oxidasePRO_0000166104Add
BLAST

Proteomic databases

MaxQBiQ06278.
PaxDbiQ06278.
PRIDEiQ06278.

PTM databases

PhosphoSiteiQ06278.

Expressioni

Tissue specificityi

Abundant in liver, expressed in adipose tissue and at lower levels in lung, skeletal muscle, pancreas. In contrast to mice, no significant gender difference in AOX1 expression level (at protein level).7 Publications

Developmental stagei

Not detected in preadipocytes but strongly induced in mature adipocytes.1 Publication

Inductioni

In liver, is down-regulated by adiponectin and by the PPARA agonist, fenofibric acid.5 Publications

Gene expression databases

ArrayExpressiQ06278.
BgeeiQ06278.
CleanExiHS_AOX1.
GenevestigatoriQ06278.

Organism-specific databases

HPAiHPA040199.
HPA040215.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi106813. 5 interactions.
IntActiQ06278. 4 interactions.
STRINGi9606.ENSP00000363832.

Structurei

3D structure databases

ProteinModelPortaliQ06278.
SMRiQ06278. Positions 4-166.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 92882Fe-2S ferredoxin-typeAdd
BLAST
Domaini236 – 421186FAD-binding PCMH-typeAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4630.
HOGENOMiHOG000191197.
HOVERGENiHBG004182.
KOiK00157.
OMAiWACRTNL.
OrthoDBiEOG7QRQSZ.
PhylomeDBiQ06278.
TreeFamiTF353036.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06278-1 [UniParc]FASTAAdd to Basket

« Hide

MDRASELLFY VNGRKVIEKN VDPETMLLPY LRKKLRLTGT KYGCGGGGCG     50
ACTVMISRYN PITKRIRHHP ANACLIPICS LYGAAVTTVE GIGSTHTRIH 100
PVQERIAKCH GTQCGFCTPG MVMSIYTLLR NHPEPTLDQL TDALGGNLCR 150
CTGYRPIIDA CKTFCKTSGC CQSKENGVCC LDQGINGLPE FEEGSKTSPK 200
LFAEEEFLPL DPTQELIFPP ELMIMAEKQS QRTRVFGSER MMWFSPVTLK 250
ELLEFKFKYP QAPVIMGNTS VGPEVKFKGV FHPVIISPDR IEELSVVNHA 300
YNGLTLGAGL SLAQVKDILA DVVQKLPEEK TQMYHALLKH LGTLAGSQIR 350
NMASLGGHII SRHPDSDLNP ILAVGNCTLN LLSKEGKRQI PLNEQFLSKC 400
PNADLKPQEI LVSVNIPYSR KWEFVSAFRQ AQRQENALAI VNSGMRVFFG 450
EGDGIIRELC ISYGGVGPAT ICAKNSCQKL IGRHWNEQML DIACRLILNE 500
VSLLGSAPGG KVEFKRTLII SFLFKFYLEV SQILKKMDPV HYPSLADKYE 550
SALEDLHSKH HCSTLKYQNI GPKQHPEDPI GHPIMHLSGV KHATGEAIYC 600
DDMPLVDQEL FLTFVTSSRA HAKIVSIDLS EALSMPGVVD IMTAEHLSDV 650
NSFCFFTEAE KFLATDKVFC VGQLVCAVLA DSEVQAKRAA KRVKIVYQDL 700
EPLILTIEES IQHNSSFKPE RKLEYGNVDE AFKVVDQILE GEIHMGGQEH 750
FYMETQSMLV VPKGEDQEMD VYVSTQFPKY IQDIVASTLK LPANKVMCHV 800
RRVGGAFGGK VLKTGIIAAV TAFAANKHGR AVRCVLERGE DMLITGGRHP 850
YLGKYKAGFM NDGRILALDM EHYSNAGASL DESLFVIEMG LLKMDNAYKF 900
PNLRCRGWAC RTNLPSNTAF RGFGFPQAAL ITESCITEVA AKCGLSPEKV 950
RIINMYKEID QTPYKQEINA KNLIQCWREC MAMSSYSLRK VAVEKFNAEN 1000
YWKKKGLAMV PLKFPVGLGS RAAGQAAALV HIYLDGSVLV THGGIEMGQG 1050
VHTKMIQVVS RELRMPMSNV HLRGTSTETV PNANISGGSV VADLNGLAVK 1100
DACQTLLKRL EPIISKNPKG TWKDWAQTAF DESINLSAVG YFRGYESDMN 1150
WEKGEGQPFE YFVYGAACSE VEIDCLTGDH KNIRTDIVMD VGCSINPAID 1200
IGQIEGAFIQ GMGLYTIEEL NYSPQGILHT RGPDQYKIPA ICDMPTELHI 1250
ALLPPSQNSN TLYSSKGLGE SGVFLGCSVF FAIHDAVSAA RQERGLHGPL 1300
TLNSPLTPEK IRMACEDKFT KMIPRDEPGS YVPWNVPI 1338
Length:1,338
Mass (Da):147,918
Last modified:November 25, 2008 - v2
Checksum:i2AB5E543F18C9261
GO

Sequence cautioni

The sequence AAA96650.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.
The sequence AAB83966.1 differs from that shown. Reason: Frameshift at positions 284, 286, 294 and 302.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti314 – 3141Q → R.
Corresponds to variant rs58185012 [ dbSNP | Ensembl ].
VAR_061136
Natural varianti802 – 8021R → C Decreases homodimerization but nearly no effect on kinetic parameters. 1 Publication
Corresponds to variant rs41309768 [ dbSNP | Ensembl ].
VAR_047517
Natural varianti921 – 9211R → H Increases homodimerization; abolishes enzymatic activity on phenanthridine; decreases turnover number with benzaldehyde, phtalazine and chloroquinazolinone as substrate, while nearly no effect on the KM. 1 Publication
Corresponds to variant rs56199635 [ dbSNP | Ensembl ].
VAR_070256
Natural varianti1135 – 11351N → S Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 Publication
Corresponds to variant rs55754655 [ dbSNP | Ensembl ].
VAR_070257
Natural varianti1271 – 12711S → L.1 Publication
Corresponds to variant rs141786030 [ dbSNP | Ensembl ].
VAR_070258
Natural varianti1297 – 12971H → R Increases homodimerization and turnover number with phenanthridine as substrate; nearly no effect on kinetic parameters with benzaldehyde, phtalazine and chloroquinazolinone as substrate. 1 Publication
Corresponds to variant rs3731722 [ dbSNP | Ensembl ].
VAR_047518

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411K → P in AAA96650. 1 Publication
Sequence conflicti41 – 411K → P in AAB83966. 1 Publication
Sequence conflicti127 – 1271T → P in AAA96650. 1 Publication
Sequence conflicti127 – 1271T → P in AAB83966. 1 Publication
Sequence conflicti152 – 1521T → H in AAA96650. 1 Publication
Sequence conflicti152 – 1521T → H in AAB83966. 1 Publication
Sequence conflicti227 – 2271E → D in AAA96650. 1 Publication
Sequence conflicti227 – 2271E → D in AAB83966. 1 Publication
Sequence conflicti251 – 2511E → D in AAA96650. 1 Publication
Sequence conflicti418 – 4181Y → I in AAA96650. 1 Publication
Sequence conflicti418 – 4181Y → I in AAB83966. 1 Publication
Sequence conflicti501 – 5011V → L in AAB83966. 1 Publication
Sequence conflicti627 – 6271I → N in AAB83966. 1 Publication
Sequence conflicti929 – 9291A → V in AAA96650. 1 Publication
Sequence conflicti929 – 9291A → V in AAB83966. 1 Publication
Sequence conflicti1019 – 10191G → A in AAA96650. 1 Publication
Sequence conflicti1019 – 10191G → A in AAB83966. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11005 mRNA. Translation: AAA96650.1. Frameshift.
AF017060
, AF009441, AF009442, AF009443, AF009444, AF009445, AF009446, AF009447, AF009448, AF009449, AF009450, AF009451, AF009452, AF009453, AF009454, AF009455, AF009456, AF009457, AF009458, AF009459, AF009460, AF009461, AF009462, AF009463, AF009464, AF009465, AF009466, AF009467, AF009468, AF009469, AF009470, AF009471, AF009472, AF009473, AF009474 Genomic DNA. Translation: AAB83966.1. Frameshift.
AF010260 Genomic DNA. Translation: AAB83968.1.
AB046692 mRNA. Translation: BAB40305.1.
AC007163 Genomic DNA. Translation: AAX93285.1.
AC080164 Genomic DNA. Translation: AAY24265.1.
CH471063 Genomic DNA. Translation: EAW70209.1.
BC117179 mRNA. Translation: AAI17180.1.
BC117181 mRNA. Translation: AAI17182.1.
CCDSiCCDS33360.1.
PIRiA49634.
RefSeqiNP_001150.3. NM_001159.3.
UniGeneiHs.406238.

Genome annotation databases

EnsembliENST00000374700; ENSP00000363832; ENSG00000138356.
GeneIDi316.
KEGGihsa:316.
UCSCiuc002uvx.3. human.

Polymorphism databases

DMDMi215273968.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11005 mRNA. Translation: AAA96650.1 . Frameshift.
AF017060
, AF009441 , AF009442 , AF009443 , AF009444 , AF009445 , AF009446 , AF009447 , AF009448 , AF009449 , AF009450 , AF009451 , AF009452 , AF009453 , AF009454 , AF009455 , AF009456 , AF009457 , AF009458 , AF009459 , AF009460 , AF009461 , AF009462 , AF009463 , AF009464 , AF009465 , AF009466 , AF009467 , AF009468 , AF009469 , AF009470 , AF009471 , AF009472 , AF009473 , AF009474 Genomic DNA. Translation: AAB83966.1 . Frameshift.
AF010260 Genomic DNA. Translation: AAB83968.1 .
AB046692 mRNA. Translation: BAB40305.1 .
AC007163 Genomic DNA. Translation: AAX93285.1 .
AC080164 Genomic DNA. Translation: AAY24265.1 .
CH471063 Genomic DNA. Translation: EAW70209.1 .
BC117179 mRNA. Translation: AAI17180.1 .
BC117181 mRNA. Translation: AAI17182.1 .
CCDSi CCDS33360.1.
PIRi A49634.
RefSeqi NP_001150.3. NM_001159.3.
UniGenei Hs.406238.

3D structure databases

ProteinModelPortali Q06278.
SMRi Q06278. Positions 4-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106813. 5 interactions.
IntActi Q06278. 4 interactions.
STRINGi 9606.ENSP00000363832.

Chemistry

BindingDBi Q06278.
ChEMBLi CHEMBL3257.
DrugBanki DB00484. Brimonidine.
DB00477. Chlorpromazine.
DB00426. Famciclovir.
DB00170. Menadione.
DB00563. Methotrexate.
DB00157. NADH.
DB00377. Palonosetron.
DB00299. Penciclovir.
DB00481. Raloxifene.
DB00962. Zaleplon.
DB00909. Zonisamide.

PTM databases

PhosphoSitei Q06278.

Polymorphism databases

DMDMi 215273968.

Proteomic databases

MaxQBi Q06278.
PaxDbi Q06278.
PRIDEi Q06278.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374700 ; ENSP00000363832 ; ENSG00000138356 .
GeneIDi 316.
KEGGi hsa:316.
UCSCi uc002uvx.3. human.

Organism-specific databases

CTDi 316.
GeneCardsi GC02P201450.
H-InvDB HIX0029780.
HGNCi HGNC:553. AOX1.
HPAi HPA040199.
HPA040215.
MIMi 602841. gene.
neXtProti NX_Q06278.
PharmGKBi PA24842.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4630.
HOGENOMi HOG000191197.
HOVERGENi HBG004182.
KOi K00157.
OMAi WACRTNL.
OrthoDBi EOG7QRQSZ.
PhylomeDBi Q06278.
TreeFami TF353036.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000138356-MONOMER.
Reactomei REACT_25012. Vitamins B6 activation to pyridoxal phosphate.
SABIO-RK Q06278.

Miscellaneous databases

ChiTaRSi AOX1. human.
GeneWikii Aldehyde_oxidase_1.
GenomeRNAii 316.
NextBioi 1283.
PROi Q06278.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q06278.
Bgeei Q06278.
CleanExi HS_AOX1.
Genevestigatori Q06278.

Family and domain databases

Gene3Di 1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProi IPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR014313. Aldehyde_oxidase.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
[Graphical view ]
Pfami PF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsi TIGR02969. mam_aldehyde_ox. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase."
    Wright R.M., Vaitaitis G.M., Wilson C.M., Repine T.B., Terada L.S., Repine J.E.
    Proc. Natl. Acad. Sci. U.S.A. 90:10690-10694(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Molecular cloning, refined chromosomal mapping, and structural analysis of the human gene encoding aldehyde oxidase (AOX1), a candidate for the ALS2 gene."
    Wright R.M., Weigel L.K., Varella-Garcia M., Vaitaitis G., Repine J.E.
    Redox Rep. 3:135-144(1997)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Mutation of human molybdenum cofactor sulfurase gene is responsible to classical xanthinuria type II."
    Ichida K., Matsumura T., Sakuma R., Hosoya T., Nishino T.
    Biochem. Biophys. Res. Commun. 282:1194-1200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  7. "Substrate specificity of human liver aldehyde oxidase toward substituted quinazolines and phthalazines: a comparison with hepatic enzyme from guinea pig, rabbit, and baboon."
    Beedham C., Critchley D.J., Rance D.J.
    Arch. Biochem. Biophys. 319:481-490(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE, SUBSTRATE SPECIFICITY.
  8. "In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver."
    Rashidi M.R., Smith J.A., Clarke S.E., Beedham C.
    Drug Metab. Dispos. 25:805-813(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Aldehyde oxidase 1 is highly abundant in hepatic steatosis and is down-regulated by adiponectin and fenofibric acid in hepatocytes in vitro."
    Neumeier M., Weigert J., Schaeffler A., Weiss T.S., Schmidl C., Buettner R., Bollheimer C., Aslanidis C., Schoelmerich J., Buechler C.
    Biochem. Biophys. Res. Commun. 350:731-735(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "Mammalian aldehyde oxidases: genetics, evolution and biochemistry."
    Garattini E., Fratelli M., Terao M.
    Cell. Mol. Life Sci. 65:1019-1048(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, NOMENCLATURE, TISSUE SPECIFICITY.
  11. "Small-interference RNA-mediated knock-down of aldehyde oxidase 1 in 3T3-L1 cells impairs adipogenesis and adiponectin release."
    Weigert J., Neumeier M., Bauer S., Mages W., Schnitzbauer A.A., Obed A., Groeschl B., Hartmann A., Schaeffler A., Aslanidis C., Schoelmerich J., Buechler C.
    FEBS Lett. 582:2965-2972(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
  12. "In vitro-in vivo correlation for intrinsic clearance for drugs metabolized by human aldehyde oxidase."
    Zientek M., Jiang Y., Youdim K., Obach R.S.
    Drug Metab. Dispos. 38:1322-1327(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  13. "Characterization of aldehyde oxidase enzyme activity in cryopreserved human hepatocytes."
    Hutzler J.M., Yang Y.S., Albaugh D., Fullenwider C.L., Schmenk J., Fisher M.B.
    Drug Metab. Dispos. 40:267-275(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, ENZYME REGULATION, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY.
  14. "Hydralazine as a selective probe inactivator of aldehyde oxidase in human hepatocytes: estimation of the contribution of aldehyde oxidase to metabolic clearance."
    Strelevitz T.J., Orozco C.C., Obach R.S.
    Drug Metab. Dispos. 40:1441-1448(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, ENZYME REGULATION, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY.
  15. Cited for: REVIEW.
  16. "Evidence for substrate-dependent inhibition profiles for human liver aldehyde oxidase."
    Barr J.T., Jones J.P.
    Drug Metab. Dispos. 41:24-29(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AZAHETEROCYCLE OXIDASE, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
  17. "Aldehyde oxidase 1 (AOX1) in human liver cytosols: quantitative characterization of AOX1 expression level and activity relationship."
    Fu C., Di L., Han X., Soderstrom C., Snyder M., Troutman M.D., Obach R.S., Zhang H.
    Drug Metab. Dispos. 41:1797-1804(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS DRUG-METABOLIZING ENZYME, SUBSTRATE SPECIFICITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "The impact of single nucleotide polymorphisms on human aldehyde oxidase."
    Hartmann T., Terao M., Garattini E., Teutloff C., Alfaro J.F., Jones J.P., Leimkuehler S.
    Drug Metab. Dispos. 40:856-864(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYS-802; HIS-921; SER-1135; LEU-1271 AND ARG-1297, CHARACTERIZATION OF VARIANTS CYS-802; HIS-921; SER-1135 AND ARG-1297, FUNCTION AS OXIDASE, HOMODIMER, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiAOXA_HUMAN
AccessioniPrimary (citable) accession number: Q06278
Secondary accession number(s): O14765
, Q53RR8, Q53TV3, Q9BYF0, Q9UPG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

AOX genes evolved from a xanthine oxidoreductase ancestral precursor via a series of gene duplication and suppression/deletion events. Different animal species contain a different complement of AOX genes encoding an equivalent number of AOX isoenzymes. In mammals, the two extremes are represented by certain rodents such as mice and rats, which are endowed with 4 AOX genes, and by humans, whose genome is characterized by a single active gene (1 Publication).

Caution

Was originally (1 Publication) thought to be a xanthine dehydrogenase.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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