A mutant adenine phosphoribosyltransferase in 2,8-dihydroxyadenine urolithiasis.
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 degrees C than control. It seems that erythrocyte adenine phosphoribosyltransferase obtained from the patient may be a variant enzyme.
D000225:Adenine / Q000031:analogs & derivatives* / Q000032:analysis; D000228:Adenine Phosphoribosyltransferase / Q000172:deficiency / Q000235:genetics*; D000328:Adult; D004912:Erythrocytes / Q000201:enzymology; D014644:Genetic Variation; D006801:Humans; D007669:Kidney Calculi / Q000032:analysis* / Q000235:genetics; D008297:Male; D010430:Pentosyltransferases / Q000235:genetics*
C002993:2,8-dihydroxyadenine; D010430:Pentosyltransferases; D000228:Adenine Phosphoribosyltransferase; D000225:Adenine