Table 2 Apparent second-order reaction rate kinetic 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

 

kcat/KM (mM-1 s-1)a

Substrate

WTb

E220A

(1,3;1,6)-β-d-Glucan (laminarin)c

234.0 ± 41.0

ndd

(1,4;1,3)-β-d-Glucan (barley glucan)c

365.5 ± 58.0

nd

Laminaribiose

41.2 ± 5.6

2.9 ± 0.1

Cellobiose

3.7 ± 0.2

0.2 ± 0.03

4NP-Glc

13.9 ± 0.6

1.3 ± 0.2

  1. aData, expressed in one or two significant digits, are given as mean values with standard error of measurements (n = 4–6) after ± signs.
  2. bFrom ref. 22.
  3. cMain types linkages and the ratio of linkage type84.
  4. dnd, (activity) not detected.
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