title: Catalytic Promiscuity of Transaminases: Preparation of Enantioenriched β-Fluoroamines by Formal Tandem Hydrodefluorination/Deamination.
abstract: Transaminases are valuable enzymes for industrial biocatalysis and enable the preparation of optically pure amines. For these transformations they require either an amine donor (amination of ketones) or an amine acceptor (deamination of racemic amines). Herein transaminases are shown to react with aromatic β-fluoroamines, thus leading to simultaneous enantioselective dehalogenation and deamination to form the corresponding acetophenone derivatives in the absence of an amine acceptor. A series of racemic β-fluoroamines was resolved in a kinetic resolution by tandem hydrodefluorination/deamination, thus giving the corresponding amines with up to greater than 99 % ee. This protocol is the first example of exploiting the catalytic promiscuity of transaminases as a tool for novel transformations.
authors.affiliation: York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.
authors.forename: Aníbal
authors.initials: A
authors.lastname: Cuetos
authors.affiliation: Departamento de Química Orgánica e Inorgánica, University of Oviedo, Instituto Universitario de Biotecnología de Asturias, C/Julián Clavería 8, 33006, Oviedo, Spain.
authors.forename: Marina
authors.initials: M
authors.lastname: García-Ramos
authors.affiliation: Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010, Graz, Austria.
authors.forename: Eva-Maria
authors.initials: EM
authors.lastname: Fischereder
authors.affiliation: Departamento de Química Orgánica e Inorgánica, University of Oviedo, Instituto Universitario de Biotecnología de Asturias, C/Julián Clavería 8, 33006, Oviedo, Spain.|Medicines Research Centre, GlaxoSmithKline R&D Ltd, Gunnels Wood Road, Stevenage, Hertfordshire, SG1 2NY, UK.
authors.forename: Alba
authors.initials: A
authors.lastname: Díaz-Rodríguez
authors.affiliation: York Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York, YO10 5DD, UK.
authors.forename: Gideon
authors.initials: G
authors.lastname: Grogan
authors.affiliation: Departamento de Química Orgánica e Inorgánica, University of Oviedo, Instituto Universitario de Biotecnología de Asturias, C/Julián Clavería 8, 33006, Oviedo, Spain. vgs@uniovi.es.
authors.forename: Vicente
authors.initials: V
authors.lastname: Gotor
authors.affiliation: Department of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, 8010, Graz, Austria. Wolfgang.Kroutil@uni-graz.at.
authors.forename: Wolfgang
authors.identifier: http://orcid.org/0000-0002-2151-6394
authors.initials: W
authors.lastname: Kroutil
authors.affiliation: Departamento de Química Orgánica e Inorgánica, University of Oviedo, Instituto Universitario de Biotecnología de Asturias, C/Julián Clavería 8, 33006, Oviedo, Spain. lavanderaivan@uniovi.es.
authors.forename: Iván
authors.identifier: http://orcid.org/0000-0003-4857-4428
authors.initials: I
authors.lastname: Lavandera
mesh_terms: D002384:Catalysis; D018360:Crystallography, X-Ray; D003641:Deamination; D004926:Escherichia coli / Q000235:genetics; D005461:Fluorine / Q000737:chemistry*; D000637:Transaminases / Q000737:chemistry* / Q000235:genetics
chemical_list: D005461:Fluorine; D000637:Transaminases
keywords: amines; biocatalysis; enzymes; fluorine; kinetic resolution