Deracemization of α-Methylbenzylamine Using an Enzyme Obtained by In Vitro Evolution

Both the catalytic activity and enantioselectivity of the amine oxidase used in the deracemization of D,L‐α‐methylbenzylamine (see scheme) have been enhanced by in vitro evolution methods to give α‐methylbenzyamine in 77 % yield and 93 % ee.

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Bibliographic Details
Published inAngewandte Chemie (International ed.) Vol. 41; no. 17; pp. 3177 - 3180
Main Authors Alexeeva, Marina, Enright, Alexis, Dawson, Michael J, Mahmoudian, Mahmoud, Turner, Nicholas J
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 02.09.2002
WILEY-VCH Verlag
WILEY‐VCH Verlag
Subjects
Amine Oxidase (Copper-Containing) - chemical synthesis
Amine Oxidase (Copper-Containing) - chemistry
amino acids
Aspergillus niger - enzymology
Chromatography, High Pressure Liquid
Cloning, Molecular
deracemization
Directed Molecular Evolution - methods
Electrophoresis, Polyacrylamide Gel
enzyme catalysis
Escherichia coli - genetics
Escherichia coli - metabolism
Mutagenesis, Site-Directed
Oxidation-Reduction
Peptide Library
Phenethylamines - chemistry
reduction
Stereoisomerism
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Summary:Both the catalytic activity and enantioselectivity of the amine oxidase used in the deracemization of D,L‐α‐methylbenzylamine (see scheme) have been enhanced by in vitro evolution methods to give α‐methylbenzyamine in 77 % yield and 93 % ee.
Bibliography:http://dx.doi.org/10.1002/1521-3773(20020902)41:17<3177::AID-ANIE3177>3.0.CO;2-P
We are grateful to the BBSRC and GlaxoSmithKline for funding a postdoctoral fellowship (M.A.) and CASE award (A.E.). We also thank the Wellcome Trust for financial support.
ArticleID:ANIE3177
istex:93952C7F22579FE6637BEABDCAB3325AFF359968
ark:/67375/WNG-RD7B26DS-G
ISSN:1433-7851
1521-3773
DOI:10.1002/1521-3773(20020902)41:17<3177::AID-ANIE3177>3.0.CO;2-P