The Function of AOX1
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.
Protein names
Recommended name:
Aldehyde oxidaseAlternative name(s):
Aldehyde oxidase 1Azaheterocycle hydroxylase
- RS55754655 (AOX1) ??
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Top Gene-Substance Interactions
AOX1 Interacts with These Diseases
| Disease | Score |
Substances That Increase AOX1
| Substances | Interaction | Organism | Category |
Substances That Decrease AOX1
| Substances | Interaction | Organism | Category |
Conditions with Increased Gene Activity
| Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
|---|
Conditions with Decreased Gene Activity
| Condition | Change (log2fold) | Comparison | Species | Experimental variables | Experiment name |
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Technical
The following transcription factors affect gene expression:
Tissue specificity:
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).
Gene Pathways:
Induction:
In liver, is down-regulated by adiponectin and by the PPARA agonist, fenofibric acid.
Developmental stage:
Not detected in preadipocytes but strongly induced in mature adipocytes.
Caution:
Was originally thought to be a xanthine dehydrogenase.
Enzyme Regulation:
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.
Cofactor:
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Molecular Function:
- 2 Iron, 2 Sulfur Cluster Binding
- Aldehyde Oxidase Activity
- Electron Carrier Activity
- Flavin Adenine Dinucleotide Binding
- Iron Ion Binding
- Molybdopterin Cofactor Binding
- Nad Binding
- Oxidoreductase Activity, Acting On Ch-Oh Group Of Donors
- Xanthine Dehydrogenase Activity
Biological Processes:
- Inflammatory Response
- Reactive Oxygen Species Metabolic Process
- Vitamin B6 Metabolic Process
- Xanthine Catabolic Process
Drug Bank:
- Brimonidine
- Menadione
- Mercaptopurine
- Raloxifene
- Famciclovir
- Idelalisib
- Lenvatinib
- Methotrexate
- Pyrazinamide
- Zaleplon
- Allopurinol
- Aminocaproic Acid
- Zonisamide