Nitrile as Activating Group in the Asymmetric Bioreduction of -Cyanoacrylic Acids Catalyzed by Ene-Reductases

Asymmetric bioreduction of an (E)--cyano-2,4-dienoic acid derivative by ene-reductases allowed a shortened access to a precursor of pregabalin [(S)-3-(aminomethyl)-5-methylhexanoic acid] possessing the desired configuration in up to 94% conversion and >99% ee. Deuterium labelling studies showed t...

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Published inAdvanced synthesis & catalysis Vol. 356; no. 8; pp. 1878 - 1882
Main Authors Winkler, Christoph K., Clay, Dorina, Turrini, Nikolaus G., Lechner, Horst, Kroutil, Wolfgang, Davies, Simon, Debarge, Sebastien, O'Neill, Pat, Steflik, Jeremy, Karmilowicz, Mike, Wong, John W., Faber, Kurt
Format Journal Article
LanguageEnglish
Published WEINHEIM Wiley 26.05.2014
Subjects
Asymmetry
Chemistry
Chemistry, Applied
Chemistry, Organic
Conversion
Derivatives
Deuterium
Esters
Labelling
Nitriles
Physical Sciences
Precursors
Science & Technology
SITE
STEREOCONTROL
CC reduction
CRYSTAL-STRUCTURE
ENOATE REDUCTASES
biocatalysis
OLD YELLOW ENZYME
FAMILY
ALKENES
ESTERS
pregabalin
cyanoacrylates
ene-reductases
TOMATO
PENTAERYTHRITOL TETRANITRATE REDUCTASE
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Summary:Asymmetric bioreduction of an (E)--cyano-2,4-dienoic acid derivative by ene-reductases allowed a shortened access to a precursor of pregabalin [(S)-3-(aminomethyl)-5-methylhexanoic acid] possessing the desired configuration in up to 94% conversion and >99% ee. Deuterium labelling studies showed that the nitrile moiety was the preferred activating/anchor group in the active site of the enzyme over the carboxylic acid or the corresponding methyl ester.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ISSN:1615-4150
1615-4169
DOI:10.1002/adsc.201301055