title: Development of an amine dehydrogenase for synthesis of chiral amines.
abstract: A leucine dehydrogenase has been successfully altered through several rounds of protein engineering to an enantioselective amine dehydrogenase. Instead of the wild-type α-keto acid, the new amine dehydrogenase now accepts the analogous ketone, methyl isobutyl ketone (MIBK), which corresponds to exchange of the carboxy group by a methyl group to produce chiral (R)-1,3-dimethylbutylamine.
authors.affiliation: School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Petit Institute of Bioengineering and Bioscience, Atlanta, GA 30332, USA.
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Abrahamson
authors.forename: Eduardo
authors.initials: E
authors.lastname: Vázquez-Figueroa
authors.forename: Nicholas B
authors.initials: NB
authors.lastname: Woodall
authors.forename: Jeffrey C
authors.initials: JC
authors.lastname: Moore
authors.forename: Andreas S
authors.initials: AS
authors.lastname: Bommarius
mesh_terms: D000588:Amines / Q000378:metabolism*; D055162:Biocatalysis; D020134:Catalytic Domain; D007651:Keto Acids / Q000737:chemistry / Q000378:metabolism; D007659:Ketones / Q000737:chemistry / Q000378:metabolism; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D015202:Protein Engineering; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D000588:Amines; D007651:Keto Acids; D007659:Ketones; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors