3-hydroxyanthranilate oxidase
| 3-hydroxyanthranilate oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.10.3.5 | ||||||||
| CAS number | 37256-65-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
3-hydroxyanthranilate oxidase is an enzyme that catalyzes the oxidation of 3-hydroxyanthranilic acid to quinolinic acid, a key intermediate in the kynurenine pathway of tryptophan metabolism. This enzyme is classified under the oxidoreductases, specifically those acting on diphenols and related substances as donors with oxygen as the acceptor.
Function[edit | edit source]
3-hydroxyanthranilate oxidase plays a crucial role in the kynurenine pathway, which is the major route of tryptophan degradation in mammals. The enzyme facilitates the conversion of 3-hydroxyanthranilic acid into quinolinic acid, which is a precursor for the synthesis of nicotinamide adenine dinucleotide (NAD+), an essential coenzyme in cellular metabolism.
Mechanism[edit | edit source]
The enzyme catalyzes the following reaction:
- 3-hydroxyanthranilate + O₂ → quinolinic acid + H₂O₂
In this reaction, 3-hydroxyanthranilate oxidase uses molecular oxygen (O₂) to oxidize 3-hydroxyanthranilic acid, producing quinolinic acid and hydrogen peroxide (H₂O₂) as byproducts.
Clinical Significance[edit | edit source]
Dysregulation of the kynurenine pathway, and consequently the activity of 3-hydroxyanthranilate oxidase, has been implicated in several neurological disorders, including Alzheimer's disease, Huntington's disease, and Parkinson's disease. Elevated levels of quinolinic acid, a neurotoxin, can lead to excitotoxicity and neuronal damage.
Research[edit | edit source]
Research into 3-hydroxyanthranilate oxidase includes studies on its structure, function, and role in disease. Understanding the enzyme's activity and regulation could lead to therapeutic targets for diseases associated with tryptophan metabolism.
Also see[edit | edit source]
- Kynurenine pathway
- Tryptophan metabolism
- Quinolinic acid
- Nicotinamide adenine dinucleotide
- Oxidoreductase
Search WikiMD
Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD
|
WikiMD's Wellness Encyclopedia |
| Let Food Be Thy Medicine Medicine Thy Food - Hippocrates |
Translate this page: - East Asian
中文,
日本,
한국어,
South Asian
हिन्दी,
தமிழ்,
తెలుగు,
Urdu,
ಕನ್ನಡ,
Southeast Asian
Indonesian,
Vietnamese,
Thai,
မြန်မာဘာသာ,
বাংলা
European
español,
Deutsch,
français,
Greek,
português do Brasil,
polski,
română,
русский,
Nederlands,
norsk,
svenska,
suomi,
Italian
Middle Eastern & African
عربى,
Turkish,
Persian,
Hebrew,
Afrikaans,
isiZulu,
Kiswahili,
Other
Bulgarian,
Hungarian,
Czech,
Swedish,
മലയാളം,
मराठी,
ਪੰਜਾਬੀ,
ગુજરાતી,
Portuguese,
Ukrainian
Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.
Contributors: Prab R. Tumpati, MD
