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1. Carbamoyl phosphate synthetase was purified up to 45-fold from Alaska pea seedling (Pisum sativum L. cultivar Alaska). 2. The enzyme was most active with and had the lowest K(m) for l-glutamine as compared with NH(4) (+). 3. The purest preparations utilized very poorly or not at all l-asparagine and urea as nitrogen donors. 4. At saturating concentrations of components of the reaction, the K(m) for l-glutamine was 1.2x10(-4)m, and the K(m) for ATP was approx. 3.9x10(-4)m. 5. Although the enzyme was very labile, stability was improved by glutamine, asparagine, ammonium sulphate, dithiothreitol and especially l-ornithine. 6. Free ATP was markedly inhibitory, and MgATP(2-) and Mg(2+) appeared to be the actual substrates utilized. 7. Fe(2+) and Mn(2+) were also utilized, but not as readily as Mg(2+) except at low concentrations. K(+) increased activity significantly. 8. Of the four nucleotides tested (ITP, ATP, GTP and UTP) only ATP served as an effective phosphate donor.

biochemical journal. cellular aspects

Partial purification and properties of carbamoyl phosphate synthetase of Alaska pea (<i>Pisum sativum</i> L. cultivar Alaska). Purification and general properties

Partial purification and properties of carbamoyl phosphate synthetase of Alaska pea (Pisum sativum L. cultivar Alaska). Purification and general properties