Table 2 Summary of enzymatic and binding parameters of Anc4 + Loop II, its mutants, and Anc5ΔLoop I

From: Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site

Variants

Mutations

Hydrolytic activity

Antifungal activity

Binding activity

 
  

(Ua/mol) × 109

(IC50)

Bmax (μmol/g)

Kd (μM)

Anc4 + II

N/A

1.15

737 ± 7

0.57 ± 0.20

8.93 ± 5.46

Anc4 + II + A

n13H/p12K

1.09

155.9 ± 13

n.d

n.d

Anc4 + II + B

s58T

1.14

593 ± 22

n.d

n.d

Anc4 + II + C

d197R/y194F/d197R

1.32

136.2 ± 4.3

1.66 ± 0.61

4.31 ± 2.06

Anc4 + II + A + B

 

0.79

129.3 ± 5.7

n.d

n.d

Anc4 + II + A + C

 

1.44

128.8 ± 7.4

3.61 ± 0.29

3.33 ± 0.71

Anc4 + II + B + C

 

1.43

72.6 ± 10

0.76 ± 0.29

1.75 ± 0.33

Anc4 + II + A + B + C

 

1.43

63.43 ± 3.8

2.04 ± 0.04

1.59 ± 0.07

Anc5ΔI

45 subs

1.28

17.2 ± 1.9

5.93 ± 0.19

1.47 ± 0.11

  1. aOne unit of activity is defined as the enzyme activity that produced one μmol of GlcNAc per minute at 37 °C. ± indicates standard deviation between three replicates. n.d. indicates activity not detected.
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