Enzymatic Preparation of Enantiomerically Pure <i>N</i>‐alkyl Amino Acids

Abstract

The isolation of enantiomerically pure L-amino acids is now possible with a bacterial acylase from N-acylated racemic precursors 1 (R1  Me, Et, nPr; R2  Me, Et); chemical preparation of these enantiomerically pure compounds is difficult. The viability of the reaction depends on the substitution pattern at the α carbon atom, but similar aminoacylases with a still wider substrate spectrum are expected to be discovered by microbiological screening.