title: A tailor-made chimeric thiamine diphosphate dependent enzyme for the direct asymmetric synthesis of (S)-benzoins.
abstract: Thiamine diphosphate dependent enzymes are well known for catalyzing the asymmetric synthesis of chiral α-hydroxy ketones from simple prochiral substrates. The steric and chemical properties of the enzyme active site define the product spectrum. Enzymes catalyzing the carboligation of aromatic aldehydes to (S)-benzoins have not so far been identified. We were able to close this gap by constructing a chimeric enzyme, which catalyzes the synthesis of various (S)-benzoins with excellent enantiomeric excess (>99%) and very good conversion.
authors.affiliation: IBG-1: Biotechnology, Forschungszentrum Jülich GmbH, Wilhelm-Johnen-Strasse, 52425 Jülich (Germany).
authors.forename: Robert
authors.initials: R
authors.lastname: Westphal
authors.forename: Constantin
authors.initials: C
authors.lastname: Vogel
authors.forename: Carlo
authors.initials: C
authors.lastname: Schmitz
authors.forename: Jürgen
authors.initials: J
authors.lastname: Pleiss
authors.forename: Michael
authors.initials: M
authors.lastname: Müller
authors.forename: Martina
authors.initials: M
authors.lastname: Pohl
authors.forename: Dörte
authors.initials: D
authors.lastname: Rother
mesh_terms: D000091:Acetobacter / Q000201:enzymology; D000446:Aldehyde-Lyases / Q000737:chemistry / Q000378:metabolism*; D001573:Benzoin / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D011551:Pseudomonas fluorescens / Q000201:enzymology; D011767:Pyruvate Decarboxylase / Q000737:chemistry / Q000378:metabolism*; D013237:Stereoisomerism; D013835:Thiamine Pyrophosphate / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011767:Pyruvate Decarboxylase; D000446:Aldehyde-Lyases; C059416:benzaldehyde lyase; D001573:Benzoin; D013835:Thiamine Pyrophosphate
keywords: C-C coupling; asymmetric catalysis; biocatalysis; enantioselectivity; protein engineering