Directed Evolution of an Amine Oxidase Possessing both Broad Substrate Specificity and High Enantioselectivity

• Published in: Angewandte Chemie (International ed.) Vol. 42; no. 39; pp. 4807 - 4810
• Main Authors: Carr, Reuben, Alexeeva, Marina, Enright, Alexis, Eve, Tom S. C., Dawson, Michael J., Turner, Nicholas J.
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 13.10.2003; WILEY‐VCH Verlag; Wiley
• Subjects: Amine Oxidase (Copper-Containing) - chemistry; Amine Oxidase (Copper-Containing) - genetics; Amine Oxidase (Copper-Containing) - metabolism; amines; Amines - chemistry; Chemistry; Chemistry, Multidisciplinary; deracemization; directed evolution; enzymes; Evolution, Molecular; Mutation; Physical Sciences; Science & Technology; Stereoisomerism; Structure-Activity Relationship; Substrate Specificity; deracemization; ENZYME-CATALYZED REACTION; KINETIC RESOLUTION; ENANTIOMERS; STEREOCHEMISTRY; amines; enzymes; QUANTITATIVE-ANALYSES; LIPASE; RACEMIZATION; directed evolution; CHIRAL AMINES
• ISSN: 1433-7851; 1521-3773
• DOI: 10.1002/anie.200352100

Evolving enzymes: Directed evolution of the amine oxidase from Aspergillus niger, by using (S)‐α‐methylbenzylamine as the target substrate, resulted in a variant enzyme (Asn336Ser) possessing both broad substrate specificity and high S enantioselectivity towards a wide range of chiral amines (see scheme).