Phenylalanine aminomutase-catalyzed addition of ammonia to substituted cinnamic acids: a route to enantiopure alpha- and beta-amino acids.
An approach is described for the synthesis of aromatic alpha- and beta-amino acids that uses phenylalanine aminomutase to catalyze a highly enantioselective addition of ammonia to substituted cinnamic acids. The reaction has a broad scope and yields substituted alpha- and beta-phenylalanines with excellent enantiomeric excess. The regioselectivity of the conversion is determined by substituents present at the aromatic ring. A box model for the enzyme active site is proposed, derived from the influence of the hydrophobicity of substituents on the enzyme affinity toward various substrates.
Szymanski
Wiktor
W
Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
Wu
Bian
B
Weiner
Barbara
B
de Wildeman
Stefaan
S
Feringa
Ben L
BL
Janssen
Dick B
DB
D024322:Amino Acids, Aromatic / Q000138:chemical synthesis*; D000641:Ammonia / Q000737:chemistry*; D002384:Catalysis; D002934:Cinnamates / Q000737:chemistry*; D019751:Intramolecular Transferases / Q000378:metabolism*; D013237:Stereoisomerism
D024322:Amino Acids, Aromatic; D002934:Cinnamates; C029010:cinnamic acid; D000641:Ammonia; D019751:Intramolecular Transferases