Stereochemistry and kinetics of the hydration of 2-acetamido-D-glucal by beta-N-acetylhexosaminidases

Kinetic studies of the hydrolysis of 2-acetamido-D-glucal by three beta-N-acetylhexosaminidases reveal that the formation of a reversible complex acting as a transition state causes the observed tight binding. The anomeric configuration of the glucal does not change during hydrolysis. Protonation from the top face occurs during the hydration reaction, indicating that glycals with appropriate substituents can serve as intermediates in these reactions by retention of beta-glycosidase.