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. 2009 Apr 28;420(Pt 1):57–65. doi: 10.1042/BJ20082397

Table 2. Kinetic properties of purified phosphorylated AtPPC1 compared with dephosphorylated AtPPC1.

Dephospho-AtPPC1 was obtained following In vitro dephosphorylation of purified AtPPC1 with bovine PP2A as described in the Experimental section and the legend to Figure 5. Ka and IC50 values were determined using subsaturating (0.25 mM) PEP. All values were determined at pH 7.3 and represent means±S.E.M. of n=4 separate determinations. All values are given in mM.

Parameter Phospho-AtPPC1 Dephospho-AtPPC1
Km(PEP) 0.18±0.02 0.34±0.01
Ka(Glc-6-P) 0.028*±0.001 ND*
IC50(L-Asp) 1.14±0.01 0.52±0.04
IC50(L-malate)+0 mM Glc-6-P 0.68±0.04 0.30±0.03
IC50(L-malate)+0.2 mM Glc-6-P 1.5±0.04 0.61±0.01
IC50(L-malate)+2 mM Glc-6-P 9.1±0.3 5.5±0.2

*Saturating Glc-6-P elicited 1.8- and 1.2-fold increases in the activity of phospho- and dephospho-AtPPC1 respectively.

†ND, not determined. Weak Glc-6-P activation prevented accurate determination of the Ka(Glc-6-P) value of dephospho-AtPPC1.