title: A thermostable transketolase evolved for aliphatic aldehyde acceptors.
abstract: Directed evolution of the thermostable transketolase from Geobacillus stearothermophilus based on a pH-based colorimetric screening of smart libraries yielded several mutants with up to 16-fold higher activity for aliphatic aldehydes and high enantioselectivity (>95% ee) in the asymmetric carboligation step.
authors.affiliation: Institut für Organische Chemie und Biochemie, Technische Universität Darmstadt, Alarich-Weiss-Str. 4, 64287 Darmstadt, Germany. fessner@tu-darmstadt.de.
authors.forename: Dong
authors.initials: D
authors.lastname: Yi
authors.forename: Thangavelu
authors.initials: T
authors.lastname: Saravanan
authors.forename: Titu
authors.initials: T
authors.lastname: Devamani
authors.forename: Franck
authors.initials: F
authors.lastname: Charmantray
authors.forename: Laurence
authors.initials: L
authors.lastname: Hecquet
authors.forename: Wolf-Dieter
authors.initials: WD
authors.lastname: Fessner
mesh_terms: D000447:Aldehydes / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004795:Enzyme Stability; D056506:Geobacillus / Q000201:enzymology; D008954:Models, Biological; D009154:Mutation; D013237:Stereoisomerism; D013696:Temperature; D014174:Transketolase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D000447:Aldehydes; D014174:Transketolase