110989-37-2Relevant academic research and scientific papers
Racemase activity of B. cepacia lipase leads to dual-function asymmetric dynamic kinetic resolution of α-aminonitriles
Vongvilai, Pornrapee,Linder, Mats,Sakulsombat, Morakot,Svedendahl Humble, Maria,Berglund, Per,Brinck, Tore,Ramstroem, Olof
, p. 6592 - 6595 (2011/09/15)
Applaudable promiscuity: Racemase-type activity discovered for B. cepacia lipase with N-substituted α-aminonitriles is proposed to involve a C-C bond-breaking/forming mechanism in the hydrolase site of the enzyme, as supported by experimental data and calculations. This promiscuous activity in combination with the transacylation activity of the enzyme enabled the asymmetric synthesis of N-methyl α-aminonitrile amides in high yield (see scheme). Copyright
