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K m =23.5 µM V max =2.65 µmol/min/mg R 2 =0.989

A. B. K m =168.6 µM V max =3.30 µmol/min/mg R 2 =0.992. K m =23.5 µM V max =2.65 µmol/min/mg R 2 =0.989. C. D. K m =32.9 µM V max =2.30 µmol/min/mg R 2 =0.979. K m =133.4 µM V max =2.68 µmol/min/mg R 2 =0.965.

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K m =23.5 µM V max =2.65 µmol/min/mg R 2 =0.989

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  1. A. B. Km=168.6 µM Vmax=3.30 µmol/min/mg R2=0.992 Km=23.5 µM Vmax=2.65 µmol/min/mg R2=0.989 C. D. Km=32.9 µM Vmax=2.30 µmol/min/mg R2=0.979 Km=133.4 µM Vmax=2.68 µmol/min/mg R2=0.965 Supplementary Fig. S1. Kinetic characterization of MdGABA-T1Δ42 activity in the forward direction. Kinetic data from a single typical enzyme preparation were best fit by non-linear regression analysis. A) Fixed GABA (2 mM), varied pyruvate. B) Fixed pyruvate (0.2 mM), varied GABA. C) Fixed GABA (2 mM), varied glyoxylate. D) Fixed glyoxylate (0.45 mM), varied GABA. Data represent the mean ± SD; where SD is not shown, it is within the symbol.

  2. B. A. Km=84.5 µM Vmax=1.03 µmol/min/mg R2=0.985 Km=18.8 µM Vmax=0.95 µmol/min/mg R2=0.974 D. C. Km=98.4 µM Vmax=1.04 µmol/min/mg R2=0.950 Km=15.1 µM Vmax=0.83 µmol/min/mg R2=0.962 Supplementary Fig. S2. Kinetic characterization of MdGABA-T2Δ42 activity in the forward direction. Kinetic data from a single typical enzyme preparation were best fit by non-linear regression analysis. A) Fixed GABA (2 mM) varied pyruvate. B) Fixed pyruvate (0.2 mM) varied GABA. C) Fixed GABA (2 mM) varied glyoxylate. D) Fixed glyoxylate (0.45 mM) varied GABA. Data represent the mean ± SD of duplicate measurements; where SD is not shown, it is within the symbol.

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