Abstract
Urate oxidase (E.C.1.7.3.3) catalyzes the oxidation of uric acid to allantoin in most mammals with the exception of humans and certain primates. In mammals, urate oxidase is found predominantly in the liver, with little or no detectable activity in other tissues. The enzyme is associated with the peroxisome and exists as a tetramer with an apparent subunit molecular weight of 32–33 kilodaltons1. Human and great apes lack urate oxidase activity2. This is substantiated by their excretion of uric acid rather than allantoin as their end product of purine catabolism. It has been proposed that the loss of urate oxidase activity in man, is a primary factor for their failure to regulate the overproduction of serum uric acid levels, leading to the common condition of gouty arthritis3. Our interest in the cloning of the mammalian urate oxidase cDNA is associated with our interest in the regulation of purine metabolism in human. Specifically, the role played by urate oxidase in the recently developed hypoxanthine phosphoribosyltransferase (HPRT) deficient mice4, 5.
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