title: A novel chimeric amine dehydrogenase shows altered substrate specificity compared to its parent enzymes.
abstract: We created a novel chimeric amine dehydrogenase (AmDH) via domain shuffling of two parent AmDHs ('L- and F-AmDH'), which in turn had been generated from leucine and phenylalanine DH, respectively. Unlike the parent proteins, the chimeric AmDH ('cFL-AmDH') catalyzes the amination of acetophenone to (R)-methylbenzylamine and adamantylmethylketone to adamantylethylamine.
authors.affiliation: Georgia Institute of Technology, School of Chemical & Biomolecular Engineering, Parker H. Petit Building, 315 Ferst Drive, Atlanta, GA 30332-0100, USA. andreas.bommarius@chbe.gatech.edu.
authors.forename: Bettina R
authors.initials: BR
authors.lastname: Bommarius
authors.forename: Martin
authors.initials: M
authors.lastname: Schürmann
authors.forename: Andreas S
authors.initials: AS
authors.lastname: Bommarius
mesh_terms: D000586:Amination; D000588:Amines / Q000737:chemistry; D000594:Amino Acid Oxidoreductases / Q000737:chemistry* / Q000235:genetics; D007659:Ketones / Q000737:chemistry; D050803:Leucine Dehydrogenase / Q000737:chemistry* / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: D000588:Amines; D007659:Ketones; D011993:Recombinant Fusion Proteins; D000594:Amino Acid Oxidoreductases; D050803:Leucine Dehydrogenase; C022342:phenylalanine oxidase