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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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BMC Research Notes

ISSN: 1756-0500

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