Table 3 Apparent inhibition constants of recombinant HvExoI wild-type (WT) and mutant E220A forms

From: The structure and dynamics of water molecule networks underlie catalytic efficiency in a glycoside exo-hydrolase

 

Kia

Inhibitor

WT glycosylated

WT De-glycosylated

E220A De-glycosylated

G6SG-OMe Ki (M) ΔG (kJ mol−1)b

109 × 10−6  − 23.0

71 × 10−6  − 24.1

340 × 10−6 − 20.1

Glucono-δ-lactone Ki (M) ΔG (kJ mol−1)

10 × 10−6  − 29.0

8 × 10−6  − 29.6

103 × 10−6 − 23.1

2F-DNPGlc Ki (M) ΔG (kJ mol−1)

0.5 × 10−6 − 36.6

0.5 × 10−6 − 36.6

0.5 × 10−6  − 36.6

  1. aData expressed in one significant digit.
  2. bCalculated according to ∆G = −RT ln [1/Ki]85.