Date published: 2025-10-19

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Xanthine Oxidase Inhibitors

Xanthine oxidase inhibitors are a class of chemical agents designed to impede the enzymatic action of xanthine oxidase (XO), a form of xanthine oxidoreductase enzyme that catalyzes the oxidation of hypoxanthine to xanthine and further to uric acid, utilizing molecular oxygen as the electron acceptor and producing reactive oxygen species as by-products. Xanthine oxidase is a metalloflavoprotein that contains flavin adenine dinucleotide (FAD), molybdenum, and iron-sulfur clusters as cofactors, which play essential roles in its catalytic activity. Inhibitors of this enzyme are structurally diverse and exert their function by binding to the active site of xanthine oxidase, thus preventing the interaction of the enzyme with its substrates. These inhibitors can be purine analogs mimicking the structure of xanthine and hypoxanthine, or non-purine compounds that also have affinity for the active site of the enzyme. Depending on their nature, xanthine oxidase inhibitors can be either reversible, where the binding to the enzyme is non-covalent and temporary, or irreversible, where the inhibitor permanently deactivates the enzyme, often through the formation of a covalent bond.The chemistry of xanthine oxidase inhibitors is intricate due to the need to specifically target the active site of the enzyme without affecting other bodily enzymes or systems. The design of these compounds often involves creating molecules that can interact with the unique features of the xanthine oxidase active site, which includes specific amino acid residues and the enzymes metal centers. Effective inhibitors typically exhibit high affinity for the active site and are able to displace the natural substrates from their binding region, thereby halting the enzymatic process. The structural components of these inhibitors must be carefully balanced to enable them to navigate through the body to reach the enzyme while maintaining enough stability to not be prematurely metabolized before they can exert their inhibitory action. In addition to the primary interaction with the active site, these compounds may also interact with other regions of the enzyme to ensure a robust inhibition.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Morin anhydrous

480-16-0sc-205955
sc-205955A
1 g
5 g
$32.00
$51.00
1
(1)

Morin anhydrous acts as a potent inhibitor of xanthine oxidase, showcasing unique molecular interactions that disrupt the enzyme's catalytic activity. Its structure allows for specific binding to the active site, altering the enzyme's conformation and reducing the formation of reactive oxygen species. The compound exhibits notable reaction kinetics, with a competitive inhibition profile that influences metabolic pathways, thereby modulating purine metabolism and oxidative stress responses.

Febuxostat

144060-53-7sc-207680
10 mg
$168.00
3
(1)

Febuxostat is a xanthine oxidase inhibitor for gout treatment. It reduces uric acid levels by inhibiting the activity of xanthine oxidase.

Purpurin

81-54-9sc-205822
sc-205822A
sc-205822B
sc-205822C
5 g
25 g
100 g
250 g
$46.00
$161.00
$398.00
$867.00
(0)

Purpurin functions as an effective xanthine oxidase inhibitor, characterized by its ability to form stable complexes with the enzyme. This interaction alters the enzyme's active site dynamics, leading to a decrease in uric acid production. The compound's unique structural features facilitate strong π-π stacking and hydrogen bonding, enhancing its binding affinity. Additionally, Purpurin exhibits distinct reaction kinetics, demonstrating non-competitive inhibition that impacts cellular redox balance and metabolic flux.

Allopurinol

315-30-0sc-207272
25 g
$128.00
(0)

Allopurinol is one of the most commonly used xanthine oxidase inhibitors. It is a first-line medication for gout and helps prevent the formation of uric acid crystals in joints.

Caffeic Acid

331-39-5sc-200499
sc-200499A
1 g
5 g
$31.00
$61.00
1
(2)

Caffeic acid acts as a xanthine oxidase inhibitor through its ability to interact with the enzyme's active site, disrupting substrate binding. Its phenolic structure allows for effective hydrogen bonding and hydrophobic interactions, which stabilize the enzyme-inhibitor complex. This compound exhibits mixed inhibition kinetics, influencing both the enzyme's affinity for its substrates and the overall reaction rate. Additionally, its antioxidant properties may modulate oxidative stress pathways, further impacting metabolic processes.

Allopurinol-d2

916979-34-5sc-207273
2.5 mg
$360.00
(0)

Allopurinol-d2 functions as a xanthine oxidase inhibitor by selectively binding to the enzyme's active site, altering its conformation and reducing its catalytic efficiency. The deuterated form enhances stability and alters reaction kinetics, providing insights into enzyme mechanisms. Its unique isotopic labeling allows for advanced spectroscopic studies, revealing intricate molecular interactions and dynamics. This compound's distinct behavior in metabolic pathways highlights its role in modulating purine metabolism.

Bendazac

20187-55-7sc-337553
5 g
$180.00
(0)

Bendazac acts as a xanthine oxidase inhibitor through its ability to form non-covalent interactions with the enzyme, disrupting substrate binding and altering electron transfer processes. Its unique structural features facilitate specific interactions with key amino acid residues, influencing the enzyme's catalytic activity. The compound's kinetic profile reveals a competitive inhibition mechanism, providing insights into the regulation of purine degradation pathways and the modulation of reactive oxygen species.