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A Biocatalyst for the Preparation of ( R ) and ( S )‐2‐Hydroxycarboxylic Acids
Author(s) -
Skopan Haike,
Günther Helmut,
Simon Helmut
Publication year - 1987
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.198701281
Subject(s) - biocatalysis , enantiomer , chemistry , proteus vulgaris , dehydrogenation , resolution (logic) , enzyme , organic chemistry , enantiomeric excess , catalysis , enantioselective synthesis , stereochemistry , biochemistry , reaction mechanism , escherichia coli , artificial intelligence , computer science , gene
“Biocatalytic enantiomer resolution of 2‐hydroxycarboxylic acids”, rac ‐1 , has been achieved with the (nonisolated) 2‐oxoacid reductase from Proteus vulgaris . This enzyme is usually employed to reduce 2‐oxomonocarboxylic acids to ( R )‐2‐hydroxycarboxylic acids (> 99% ee) with methyl‐ or benzylviologen as electron mediator. The use of carbamoylmethylviologen has allowed, for the first time, the reverse reaction to be carried out. Only the ( R ) enantiomer of rac ‐ 1 undergoes dehydrogenation; the ( S )‐2‐hydroxycarboxylic acid remains unchanged. The mediator can be regenerated.