Dynamic Kinetic Resolution for Asymmetric Synthesis of L‐Noncanonical Amino Acids from D‐Ser Using Tryptophan Synthase and Alanine Racemase.

L‐Ser is often used to synthesize some significant l‐noncanonical α‐amino acids(l‐ncAAs), which are the prevalent intermediates and precursors for functional synthetic compounds. In this study, threonine aldolase from Escherichia coli k‐12 MG1655 has been used to synthesize l‐Ser. In contrast to the maximum catalytic capacity (20 g/L) for l‐threonine aldolase(LTA), d‐Ser was synthesized with high yield (240 g/L) from cheap Gly and paraformaldehyde using d‐threonine aldolase (DTA) from Arthrobacter sp ATCC. In order to fully utilize d‐Ser and expand the resource of l‐Ser, a dynamic kinetic resolution system was constructed to convert d/dl‐Ser to l‐Ser through combining alanine racemase (Alr) from Bacillus subtilis with l‐tryptophan synthase (TrpS) from Escherichia coli k‐12 MG1655, and l‐ncAAs including l‐Trp and l‐Cys derivatives were synthesized with excellent enantioselectivity and in high yields. The results indicated l‐ncAAs could be efficiently synthesized from d‐Ser using this original and green dynamic kinetic resolution system, and the reliable l‐Ser resource has been established from simple and achiral substrates. [ABSTRACT FROM AUTHOR]