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Table 1 Apparent steady-state kinetic parameters and equilibrium binding constants for wild type and K69A mutant Mtb SD

From: The conserved Lysine69 residue plays a catalytic role in Mycobacterium tuberculosis shikimate dehydrogenase

Parameter Wild-type K69A
Vmax (U mg-1)a 110 ± 2 1.61 ± 0.03
Km DHS (μM)a 29 ± 2 76 ± 4
Km NADPH (μM)a 11.0 ± 0.6 30 ± 2
kcat (s-1)a 50 ± 1 0.73 ± 0.01
kcat/Km DHS (M-1 s-1)a 1.7 (± 0.1) × 106 9.6 (± 0.5) × 103
kcat/Km NADPH (M-1 s-1)a 4.5 (± 0.2) × 106 24 (± 2) × 103
Kd DHS (μM)b 32 ± 4 134 ± 21
  1. a steady-state kinetic parameters
  2. b spectroscopic measurements of intrinsic protein fluorescence (equilibrium binding)
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