Chemoenzymatic dynamic kinetic resolution.
During the past decade a new concept has appeared in asymmetric catalysis involving the combination of a biocatalyst and a chemocatalyst in one 'pot' leading to efficient deracemization via dynamic kinetic resolution (DKR). Here, we outline the different strategies that have been developed for efficient chemoenzymatic DKR, in particular the powerful combination of an enzyme and a metal catalyst.
Pàmies
Oscar
O
Department of Physical and Inorganic Chemistry, Rovira i Virgili University, Pl. Imperial Tarraco 1, 43005 Tarragona, Spain.
Bäckvall
Jan-E
JE
D001711:Biotransformation; D016956:Burkholderia cepacia / Q000201:enzymology; D002384:Catalysis; D002625:Chemistry, Organic / Q000379:methods; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D004951:Esterification; D005656:Fungal Proteins; D006859:Hydrogen / Q000737:chemistry; D007700:Kinetics; D008049:Lipase / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010165:Palladium / Q000737:chemistry; D012428:Ruthenium / Q000737:chemistry; D013237:Stereoisomerism; D013379:Substrate Specificity
D004798:Enzymes; D005656:Fungal Proteins; D010165:Palladium; D012428:Ruthenium; D006859:Hydrogen; D008049:Lipase; C431349:lipase B, Candida antarctica