Search Results
Overview
| Uniprot ID | Q06278 |
|---|---|
| Protein Name | Aldehyde oxidase |
| Gene Name | AOX1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1003 | FNAENYWKKKGLAMV |
| 1108 | DACQTLLKRLEPIIS |
| 1116 | RLEPIISKNPKGTWK |
| 1119 | PIISKNPKGTWKDWA |
| 1321 | ACEDKFTKMIPRDEP |
| 166 | DACKTFCKTSGCCQS |
| 258 | ELLEFKFKYPQAPVI |
| 278 | VGPEVKFKGVFHPVI |
| 330 | VQKLPEEKTQMYHAL |
| 421 | VNIPYSRKWEFVSAF |
| 474 | GPATICAKNSCQKLI |
| 479 | CAKNSCQKLIGRHWN |
| 559 | ALEDLHSKHHCSTLK |
| 566 | KHHCSTLKYQNIGPK |
| 722 | SSFKPERKLEYGNVD |
| 790 | DIVASTLKLPANKVM |
| 795 | TLKLPANKVMCHVRR |
| 810 | VGGAFGGKVLKTGII |
| 854 | GRHPYLGKYKAGFMN |
| 856 | HPYLGKYKAGFMNDG |
| 949 | KCGLSPEKVRIINMY |
| 957 | VRIINMYKEIDQTPY |
| 965 | EIDQTPYKQEINAKN |
| 995 | LRKVAVEKFNAENYW |
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. May also 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
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070062 | extracellular exosome |
| Molecular Function | GO:0051537 | 2 iron, 2 sulfur cluster binding |
| Molecular Function | GO:0004031 | aldehyde oxidase activity |
| Molecular Function | GO:0071949 | FAD binding |
| Molecular Function | GO:0050660 | flavin adenine dinucleotide binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0005506 | iron ion binding |
| Molecular Function | GO:0043546 | molybdopterin cofactor binding |
| Molecular Function | GO:0051287 | NAD binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Biological Process | GO:0006629 | lipid metabolic process |
| Biological Process | GO:0006805 | xenobiotic metabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.