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Figure 4 | BMC Biochemistry

Figure 4

From: Integrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase – aspartate transcarbamylase multifunctional protein

Figure 4

Substrate saturation curves of the CPSase from the mutant Glu 2182→Lys in presence or absence of UTP. The CPSase activity was measured as indicated in the Methods. On the left are represented the double reciprocal plots in the presence of () 0 mM, () 3 mM, and (■) 6 mM UTP. On the right are presented the corresponding Dixon plots. The concentrations used were () 6.7 mM, () 9.3 mM, (■) 10.7 mM, and () 33 mM in the case of ATP; () 2.1 mM, () 5.3 mM, (■) 7.5 mM, and () 20 mM in the case of bicarbonate; () 0.03 mM, () 0.07 mM, (■) 0.3 mM, and () 1 mM in the case of glutamine.

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