TABLE 3.
Summary of the demonstrated activities of BglF domain polypeptides
| BglF domain(s) | β-Glucoside phosphory-lationa | BglG phosphory-lationb | BglG dephosphory-lationc |
|---|---|---|---|
| BCA (wild-type BglF) | + | + | + |
| A | − | − | − |
| B | − | + | − |
| C | − | − | − |
| CA | − | − | − |
| BC | + | + | + |
| C + B | − | + | − |
a
Ability to phosphorylate β-glucosides in vitro (Fig. 3) and/or to complement bglF mutant strains (Table 2).
b
Ability to phosphorylate BglG in vitro (Fig. 4) and/or to negatively regulate BglG activity in vivo (Table 2, β-galactosidase activity without salicin).
c
Ability to restore BglG activity in vivo in the presence of β-glucosides (Table 2, β-galactosidase activity with salicin).