[9] Oxygen accepts two electrons from the urate dianion, via a sequence of one-electron transfers, ultimately yielding hydrogen peroxide and the dehydrogenated substrate.

[12] Genetically, the loss of urate oxidase function in humans was caused by two nonsense mutations at codons 33 and 187 and an aberrant splice site.

[13] It has been proposed that the loss of urate oxidase gene expression has been advantageous to hominoids, since uric acid is a powerful antioxidant and scavenger of singlet oxygen and radicals.

Its presence provides the body with protection from oxidative damage, thus prolonging life and decreasing age-specific cancer rates.

[12] Urate oxidase is formulated as a protein drug (rasburicase) for the treatment of acute hyperuricemia in patients receiving chemotherapy.

A PEGylated form of urate oxidase, pegloticase, was FDA approved in 2010 for the treatment of chronic gout in adult patients refractory to "conventional therapy".

[16] Children with non-Hodgkin's lymphoma (NHL), specifically with Burkitt's lymphoma and B-cell acute lymphoblastic leukemia (B-ALL), often experience tumor lysis syndrome (TLS), which occurs when breakdown of tumor cells by chemotherapy releases uric acid and cause the formation of uric acid crystals in the renal tubules and collecting ducts.

[21] Urate oxidase is a notable example of the existence of non-homologous isofunctional enzymes, proteins with independent evolutionary origin catalyzing the same chemical reaction.