Carbamylphosphate synthetase from Salmonella typhimurium. Regulations, subunit composition, and function of the subunits.

@article{Abdelal1975CarbamylphosphateSF,
  title={Carbamylphosphate synthetase from Salmonella typhimurium. Regulations, subunit composition, and function of the subunits.},
  author={A. Abdelal and John L. Ingraham},
  journal={The Journal of biological chemistry},
  year={1975},
  volume={250 12},
  pages={4410-7}
}
Carbamylphosphate synthetase was purified to homogeneity from a derepressed strain of Salmonella typhimurium by a procedure based on affinity chromatography employing immobilized glutamine. The enzyme catalyzes the synthesis of carbamylphosphate from either ammonia or glutamine together with ATP and bicarbonate. The ATP saturation curve of either nitrogen donor is sigmoidal (n equals 1.5) but the affinity for ATP is higher with ammonia. In addition to the feedback inhibition by UMP and… CONTINUE READING

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