Abstract
Both optically pure enantiomers of N-hydroxymethyl vince lactam are the key synthons for some important antiviral drugs. The high enantioselective transesterification of N-hydroxymethyl vince lactam was catalyzed by the lipase from Burkholderia ambifaria YCJ01 using vinyl acetate as the acyl donor. Under the optimized conditions, an efficient resolution of N-hydroxymethyl vince lactam in high substrate concentration (300mM; 41.7g/L) was obtained with nearly theoretical conversion yield of 50.1%, eep of 99% and ees of 99%. Strikingly, the highest enantioselectivity (E>900) and dramatic increase of the lipase activity towards N-hydroxymethyl vince lactam were observed in a binary solvent system with hexane and MTBE (v/v=1:9). The high substrate tolerance and enantioselectivity of lipase YCJ01 showed significant benefit in the practical resolution of racemic N-hydroxymethyl vince lactam. Additionally, the high enantiopreference of lipase YCJ01 towards (−)-N-hydroxymethyl vince lactam was also rationalized through molecular docking.
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