Regulatory properties of carbamoyl-phosphate synthetase II from the parasitic protozoan Crithidia fasciculata.
1. At the lowered concentrations of 0.5 mM ATP and 1.5 mM MgCl2, 2.0 mM UTP, UDP and UMP inhibited the activity of Crithidia fasciculata carbamoyl-phosphate synthetase II by about 65, 80 and 40% respectively. 2. The result suggests that feedback inhibition of the activity by uridine nucleotides is a mechanism of regulation of the de novo pyrimidine biosynthetic pathway in C. fasciculata. 3. ADP, AMP and CDP inhibited the activity (about 70, 40 and 40%). 4. Excess Mg2+ at around 1 mM, relative to the ATP concentration, was required for the maximum activity. 5. 5-Phosphoribosyl 1-pyrophosphate had no significant effect on the activity under various conditions examined.
D000818:Animals; D002223:Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing) / Q000378:metabolism*; D003421:Crithidia / Q000201:enzymology*; D005246:Feedback; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D010754:Phosphoribosyl Pyrophosphate / Q000494:pharmacology; D012265:Ribonucleotides / Q000494:pharmacology
D012265:Ribonucleotides; D010754:Phosphoribosyl Pyrophosphate; D008025:Ligases; D002223:Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)