Xanthine oxidase

Xanthine oxidase (syn. hypoxanthine oxidase) is an enzyme that plays an important role in the metabolism of purines in the body. This enzyme is involved in the metabolism of uric acid, which is the end product of the breakdown of purine nucleotides.

Xanthine oxidase catalyzes the oxidative deamination of purine bases to produce uric acid and nitric oxide. This enzyme is also involved in the regulation of uric acid levels in the blood, as it can oxidize both excess and deficient uric acid, thereby regulating its levels.

In addition, xanthine oxidase plays an important role in protecting the body from the toxic effects of uric acid. It can bind excess uric acid levels to form non-toxic compounds such as alloxanthin and alloxazine. This helps prevent the accumulation of uric acid in tissues and organs, which can lead to various diseases.

The importance of xanthine oxidase in purine metabolism and regulation of uric acid levels makes it a key enzyme in purine metabolism. Impaired function of this enzyme can lead to the development of various diseases associated with impaired purine metabolism, such as gout and hyperuricemia.

In conclusion, xanthine oxidase is an important enzyme involved in purine metabolism and regulating uric acid levels in the body. Its disruption can lead to serious illness, so it is important to understand its role in the body and monitor its function.



A xanthine oxidase enzyme that catalyzes the oxidoreduction of xanthine into hypoxanthine and then into uric acid. In all cells containing guanosine nucleotides in humans and animals (except embryos), other enzymes of the oxidase series are also found - guanine deaminase; adenine phosphoribosyltransferase (synthesis of adenylic acid).

Xanthine oxidases are soluble, leachable mitochondrial proteins; There are 3 isoenzymes present in human plasma, of which the α-forms are polymorphic. The oxidation reaction occurs in an acidic environment of 7-7.5 pH and also requires Mn2+ and is stimulated by adenosine, guanine and DPN.

The key role of such an enzyme when taking drugs with purine subgroups is associated with the formation of sodium urate. Due to treatment with quinine, patients exhibit clinical signs of leukopenia. Biochemistry.