Inactivation of a beta-glucosidase through the accumulation of a stable 2-deoxy-2-fluoro-alpha-D-glucopyranosyl-enzyme intermediate: a detailed investigation

The inactivation of Agrobacterium beta-glucosidase by 2-deoxy-2-fluoroglycoside through the accumulation of a covalent 2-deoxy-2-fluoro-alpha-D-glucopyranosyl enzyme intermediate was thoroughly investigated. Simultaneous release of aglycon during inactivation was observed. In addition, the rate of inactivation depended on the leaving group ability of the aglycon, which yields only partial inactivation due to competition between turnover and formation of intermediates. Moreover, the turnover rate was increased by transglycosylation to a suitable glycoside bound in the aglycon site, yielding a disaccharide product.