We previously reported the isolation and characterization of a bacterial deacetylase (CmCBDA), which catalyzes selectively the hydrolysis of GlcNAc to glucosamine under mild reaction conditions. This CmCBDA deacetylase was further studied and demonstrated to catalyze the N-acylation of unprotected glucosamine and to N-transacylate unprotected N-acetylglucosamine at ambient temperatures. A wide range of N-acylglucosamine derivatives bearing aliphatic chains or different functional groups suitable for further incorporation reactions were obtained in high conversion rates. Furthermore, CmCBDA catalyzed the N-acylation of glucosamine and was used in an enzymatic cascade for the synthesis of sialosides.
- Lv Y.M.; Laborda P.; Huang K.; Cai Z.P.; Wang M.; Lu A.M.; Doherthy C.; Liu L.; Flitsch S.L.; Voglmeir J. Green Chemistry 2017, 19, 527-535.