• In one case of 2,8-dihydroxyadenine urolithiasis, reduced adenine phosphoribosyltransferase activity was found. The patient's enzyme had normal affinity for adenine but reduced affinity for substrate phosphoribosyl-pyrophosphate. It was much more stable at 60°C than control. It seems that erythrocyte adenine phosphoribosyltransferase obtained from the patient may be a variant enzyme.
(Arch Intern Med 1986;146:2068-2070)
Nishida Y, Hirano S, Miyamoto T. A Mutant Adenine Phosphoribosyltransferase in 2,8-Dihydroxyadenine Urolithiasis. Arch Intern Med. 1986;146(10):2068-2070. doi:10.1001/archinte.1986.00360220250040