24593-49-5Relevant articles and documents
One-Pot Enantioselective Synthesis of d-Phenylglycines from Racemic Mandelic Acids, Styrenes, or Biobased l-Phenylalanine via Cascade Biocatalysis
Zhou, Yi,Wu, Shuke,Li, Zhi
supporting information, p. 4305 - 4316 (2017/11/21)
Enantiopure d-phenylglycine and its derivatives are an important group of chiral amino acids with broad applications in thepharmaceutical industry. However, the existing synthetic methods for d-phenylglycine mainly rely on toxic cyanide chemistry and multistep processes. To provide green and safe alternatives, we envisaged cascade biocatalysis for the one-pot synthesis of d-phenylglycine from racemic mandelic acid, styrene, and biobased l-phenylalanine, respectively. Recombinant Escherichia coli (LZ110) was engineered to coexpress four enzymes to catalyze a 3-step reaction in one pot, transforming mandelic acid (210 mM) to give enantiopure d-phenylglycine in 29.5 g L?1 (195 mM) with 93% conversion. Using the same whole-cell catalyst, twelve other d-phenylglycine derivatives were also produced from the corresponding mandelic acid derivatives in high conversion (58–94%) and very high ee (93–99%). E. coli (LZ116) expressing seven enzymes was constructed for the transformation of styrene to enantiopure d-phenylglycine in 80% conversion via a one-pot 6-step cascade biotransformation. Twelve substituted d-phenylglycines were also produced from the corresponding styrene derivatives in high conversion (45–90%) and very high ee (92–99%) via the same cascade reactions. A nine-enzymeexpressing E. coli (LZ143) was engineered to transform biobased l-phenylalanine to enantiopure d-phenylglycine in 83% conversion via a one-pot 8-step transformation. Preparative biotransformations were also demonstrated. The high-yielding synthetic methods use cheap and green reagents (ammonia, glucose, and/or oxygen), and E. coli whole-cell catalysts, thus providing green and useful alternative methods for manufacturing d-phenylglycine. (Figure presented.).
Practical and convenient enzymatic synthesis of enantiopure α-amino acids and amides
Wang, Mei-Xiang,Lin, Shuang-Jun
, p. 6542 - 6545 (2007/10/03)
Catalyzed by the nitrile hydratase and the amidease in Rhodococcus sp. AJ270 cells under very mild conditions, a number of α-aryl- and α-alkyl-substituted DL-glycine nitriles 1 rapidly underwent a highly enantioselective hydrolysis to afford D-(-)-α-amino acid amides 2 and L-(+)-α-amino acids 3 in high yields with excellent enantiomeric excesses in most cases. The overall enantioselectivity of the biotransformations of nitriles originated from the combined effects of a high L-enantioselective amidase and a low enantioselective nitrile hydratase. The influence of the substrates on both reaction efficiency and enantioselectivity was also discussed in terms of steric and electronic effects. Coupled with chemical hydrolysis of D-(-)-α-phenylglycine amide, biotransformation of DL-phenylglycine nitrile was applied in practical scale to produce both D- and L-phenylglycines in high optical purity.
Synthesis of Optically Active Arylglycines by Photolysis of Optically Active (β-Hydroxyamino) Carbene-Chromium(0) Complexes
Vernier, Jean-Michel,Hegedus, Louis S.,Miller, David B.
, p. 6914 - 6920 (2007/10/02)
Photolysis of chromium complexes having the optically active amino alcohol (1R,2S)-(-)- or (1S,2R)-(+)-2-amino-1,2-diphenylethanol as the amino group produced aryl-substituted oxazinones in good yield with reasonable diastereoselectivity.Facile separation of diastereoisomers followed by mild reductive cleavage produced several arylglycines, having either electron-donating or withdrawing groups on the aromatic ring, in good overall yield and with excellent enantiomeric excess.
