| Identification |
|---|
| HMDB Protein ID
| HMDBP12346 |
| Secondary Accession Numbers
| None |
| Name
| Aldehyde oxidase 1 |
| Synonyms
|
- Azaheterocycle hydroxylase 1
|
| 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 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. Is a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also catalyzes nitric oxide (NO) production; under anaerobic conditions, reduces nitrite to NO with NADH or aldehyde as electron donor, but under aerobic conditions, NADH is the preferred substrate. These reactions may be catalyzed by several isozymes. May play a role in adipogenesis. |
| 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 |
| xenobiotic metabolic process |
| Cellular Component |
| cytosol |
| Molecular Function |
| FAD binding |
| retinal oxidase activity |
| heptaldehyde:oxygen oxidoreductase activity |
| geranial:oxygen oxidoreductase activity |
| oxidoreductase activity |
| molybdopterin cofactor binding |
| 2 iron, 2 sulfur cluster binding |
| aldehyde oxidase activity |
| iron ion binding |
| identical protein binding |
| flavin adenine dinucleotide binding |
| protein homodimerization activity |
| NAD binding |
| electron carrier activity |
|
| 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
| 1333 |
| Molecular Weight
| 146919.64 |
| Theoretical pI
| 6.977 |
| 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
| Q9Z0U5 |
| UniProtKB/Swiss-Prot Entry Name
| AOXA_RAT |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Li H, Kundu TK, Zweier JL: Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite. J Biol Chem. 2009 Dec 4;284(49):33850-8. doi: 10.1074/jbc.M109.019125. Epub 2009 Sep 28. [PubMed:19801639 ]
- 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 ]
- Wright RM, Clayton DA, Riley MG, McManaman JL, Repine JE: cDNA cloning, sequencing, and characterization of male and female rat liver aldehyde oxidase (rAOX1). Differences in redox status may distinguish male and female forms of hepatic APX. J Biol Chem. 1999 Feb 5;274(6):3878-86. doi: 10.1074/jbc.274.6.3878. [PubMed:9920943 ]
- Kundu TK, Hille R, Velayutham M, Zweier JL: Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues. Arch Biochem Biophys. 2007 Apr 1;460(1):113-21. doi: 10.1016/j.abb.2006.12.032. Epub 2007 Jan 23. [PubMed:17353002 ]
- Hamzeh-Mivehroud M, Rahmani S, Rashidi MR, Hosseinpour Feizi MA, Dastmalchi S: Structure-based investigation of rat aldehyde oxidase inhibition by flavonoids. Xenobiotica. 2013 Aug;43(8):661-70. doi: 10.3109/00498254.2012.755228. Epub 2013 Jan 3. [PubMed:23282065 ]
|
