Asymmetric Synthesis of Enantiomerically Pure Aliphatic and Aromatic D-Amino Acids Catalyzed by Transaminase from Haliscomenobacter hydrossis

D-amino acids are valuable building blocks for the synthesis of biologically active compounds and pharmaceuticals. The asymmetric chiral amino from prochiral ketones using stereoselective enzymes is a well-known but far exhausted approach large-scale production. Herein, we investigated pyridoxal-5′-phosphate-dependent acid transaminase Haliscomenobacter hydrossis as potential biocatalyst enzymatic optically pure aliphatic aromatic acids. We studied catalytic efficiency stereoselectivity H. in amination α-keto acids, D-glutamate source group. constructed one-pot three-enzyme system, which included two auxiliary enzymes, hydroxyglutarate dehydrogenase, glucose to produce with product yield 95–99% an enantiomeric excess more than 99%. estimated stability cofactor leakage under reaction conditions. It was found that high concentration well low temperature (30 °C) can reduce obtained results demonstrated enantiomerically