| Identification |
|---|
| HMDB Protein ID
| HMDBP12345 |
| Secondary Accession Numbers
| None |
| Name
| Aldehyde oxidase 1 |
| Synonyms
|
- Azaheterocycle hydroxylase 1
- Retinal oxidase
- Retinoic acid synthase
|
| Gene Name
| AOX1 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N-methylphthalazinium and phthalazine, 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. Cannot use hypoxanthine and all-trans-retinol as substrate. |
| Pathways
|
- Drug metabolism - cytochrome P450
- JAK-STAT signaling pathway
- Nicotinate and nicotinamide metabolism
- Retinol metabolism
- Tryptophan metabolism
- Tyrosine metabolism
- Valine, leucine and isoleucine degradation
- Vitamin B6 metabolism
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| drug metabolic process |
| Cellular Component |
| cytosol |
| Molecular Function |
| electron carrier activity |
| NAD binding |
| aldehyde oxidase activity |
| 2 iron, 2 sulfur cluster binding |
| molybdopterin cofactor binding |
| iron ion binding |
| FAD binding |
| geranial:oxygen oxidoreductase activity |
| heptaldehyde:oxygen oxidoreductase activity |
| retinal oxidase activity |
| protein homodimerization activity |
| flavin adenine dinucleotide binding |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 1334 |
| Molecular Weight
| 147137.285 |
| Theoretical pI
| 6.702 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| P80456 |
| UniProtKB/Swiss-Prot Entry Name
| AOXA_RABIT |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Rashidi MR, Smith JA, Clarke SE, Beedham C: In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver. Drug Metab Dispos. 1997 Jul;25(7):805-13. [PubMed:9224775 ]
- Kurosaki M, Bolis M, Fratelli M, Barzago MM, Pattini L, Perretta G, Terao M, Garattini E: Structure and evolution of vertebrate aldehyde oxidases: from gene duplication to gene suppression. Cell Mol Life Sci. 2013 May;70(10):1807-30. doi: 10.1007/s00018-012-1229-5. Epub 2012 Dec 21. [PubMed:23263164 ]
- Huang DY, Furukawa A, Ichikawa Y: Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch Biochem Biophys. 1999 Apr 15;364(2):264-72. doi: 10.1006/abbi.1999.1129. [PubMed:10190983 ]
- Turner NA, Doyle WA, Ventom AM, Bray RC: Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase. Eur J Biochem. 1995 Sep 1;232(2):646-57. [PubMed:7556219 ]
- Tsujita M, Tomita S, Miura S, Ichikawa Y: Characteristic properties of retinal oxidase (retinoic acid synthase) from rabbit hepatocytes. Biochim Biophys Acta. 1994 Jan 11;1204(1):108-16. doi: 10.1016/0167-4838(94)90039-6. [PubMed:8305467 ]
|
