. 2016 Jul 8;11(7):e0159002. doi: 10.1371/journal.pone.0159002

Table 2. V_max and K_m values and inhibition patterns of PEPCK-C isoenzymes in the presence of glyceroneogenic substrates and compound 1.

	[Compound 1] (μM)	OAA		GTP
		V_max (μmol min^-1 mg^-1)	K_m (μM)	V_max (μmol min^-1 mg^-1)	K_m (μM)
139Met	0 μM	21.3 ± 3.7	22 ± 14	20.0 ± 1.9	96 ± 15
139Met	50 μM	6.7 ± 1.4	13 ± 5	7.8 ± 0.5	118 ± 14
139Leu	0 μM	21.8 ± 1.8 ns	14 ± 4 ns	22.5 ± 4.2 ns	99 ± 14 ns
139Leu	50 μM	9.4 ± 1.3 ns	11 ± 3 ns	7.2 ± 0.4 ns	155 ± 30 ns

Values given are the mean of three independent experiments ± SD. Differences in V_max and K_m between 139Met and 139Leu were calculated using two-sample t-test; ns: not significant.

Table 2. Vmax and Km values and inhibition patterns of PEPCK-C isoenzymes in the presence of glyceroneogenic substrates and compound 1.

Table 2. V_max and K_m values and inhibition patterns of PEPCK-C isoenzymes in the presence of glyceroneogenic substrates and compound 1.