Racemase Activity of B. cepacia Lipase Leads to Dual-Function Asymmetric Dynamic Kinetic Resolution of alpha-Aminonitriles
2011 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 50, no 29, 6592-6595 p.Article in journal (Refereed) Published
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).
Place, publisher, year, edition, pages
2011. Vol. 50, no 29, 6592-6595 p.
dynamic kinetic resolution, enzyme catalysis, racemase activity, secondary amines, Strecker reaction
IdentifiersURN: urn:nbn:se:kth:diva-37184DOI: 10.1002/anie.201007373ISI: 000292644400026ScopusID: 2-s2.0-79959992526OAI: oai:DiVA.org:kth-37184DiVA: diva2:432472
Uppdated from Manuscript to Article. QC 201209032011-08-032011-08-032012-09-03Bibliographically approved