Rudimentary locus of Drosophila melanogaster: partial purification of a carbamylphosphate synthase--aspartate transcarbamylase--dihydroorotase complex.
Glutamine-dependent CPSase, ATCase, and DHOase from Drosophila, the first three enzymes in pyrimidine biosynthesis, show coordinate variation in activity throughout development. The three activities were highest in first instar larvae and decreased as development proceeded. The three activities cosediment in sucrose gradients as a single peak with a relative sedimentation coefficient of approximately 30S. CPSase, ATCase, and DHOase copurify during (NH4)2SO4 fractionation and during DEAE-cellulose and hydroxylapatite chromatography.
D000581:Amidohydrolases / Q000235:genetics*; D000818:Animals; D001221:Aspartate Carbamoyltransferase / Q000235:genetics* / Q000302:isolation & purification; D002223:Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) / Q000235:genetics* / Q000302:isolation & purification; D004080:Dihydroorotase / Q000235:genetics* / Q000302:isolation & purification; D004331:Drosophila melanogaster / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D009097:Multienzyme Complexes / Q000235:genetics* / Q000302:isolation & purification; D010770:Phosphotransferases / Q000235:genetics*
D009097:Multienzyme Complexes; D001221:Aspartate Carbamoyltransferase; D010770:Phosphotransferases; D000581:Amidohydrolases; D004080:Dihydroorotase; D002223:Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)