|
Figure 4.
Proposed mechanisms of glucosyl transfer catalyzed by GT
retaining enzymes. Two essential components of
double-displacement, a catalytic nucleophile and a
glucosyl-enzyme intermediate, are circled and framed,
respectively. In S[n]i- and S[n]1-like mechanisms, the
positively charged DGM (framed) is stabilized by the leaving
group AMP-phosphate and the incoming nucleophile 4-hydroxyl
group of the sugar.
|