Premium
Racemase Activity of B. cepacia Lipase Leads to Dual‐Function Asymmetric Dynamic Kinetic Resolution of α‐Aminonitriles
Author(s) -
Vongvilai Pornrapee,
Linder Mats,
Sakulsombat Morakot,
Svedendahl Humble Maria,
Berglund Per,
Brinck Tore,
Ramström Olof
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201007373
Subject(s) - lipase , kinetic resolution , stereochemistry , function (biology) , enzyme , chemistry , mechanism (biology) , biochemistry , catalysis , enantioselective synthesis , biology , philosophy , epistemology , evolutionary biology
Applaudable promiscuity : Racemase‐type activity discovered for B. cepacia lipase with N‐substituted α‐aminonitriles is proposed to involve a CC 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).