Document Detail


Nitrilases catalyze key step to conformationally constrained GABA analogous gamma-amino acids in high optical purity.
MedLine Citation:
PMID:  17715966     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Five- and six-membered carbocyclic gamma-amino acids were prepared in high enantiomeric purity by nitrilase-mediated transformation of hitherto unreported gamma-amino nitriles. The nitrilases investigated reveal a strong enantiopreference for cis-isomers (up to 99% ee), whereas trans-isomers were available in up to 86% ee. The biocatalytic enantioselective syntheses of cis-3-aminocyclohexanecarboxylic acid (3b), trans-3-aminocyclohexanecarboxylic acids (4b, 6b, 8b) as well as trans-3-aminocylopentanecarboxylic acid (2b) are hereby reported for the first time.
Authors:
Margit Winkler; Astrid C Knall; Martin R Kulterer; Norbert Klempier
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Publication Detail:
Type:  Journal Article     Date:  2007-08-23
Journal Detail:
Title:  The Journal of organic chemistry     Volume:  72     ISSN:  0022-3263     ISO Abbreviation:  J. Org. Chem.     Publication Date:  2007 Sep 
Date Detail:
Created Date:  2007-09-07     Completed Date:  2007-10-16     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985193R     Medline TA:  J Org Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7423-6     Citation Subset:  IM    
Affiliation:
Institute of Organic Chemistry, Graz University of Technology, Stremayrgasse 16, A-8010 Graz, Austria.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / chemical synthesis*
Aminohydrolases / chemistry*,  metabolism
Catalysis
Hydrolysis
Stereoisomerism
gamma-Aminobutyric Acid / analogs & derivatives*
Chemical
Reg. No./Substance:
0/Amino Acids; 56-12-2/gamma-Aminobutyric Acid; EC 3.5.4.-/Aminohydrolases; EC 3.5.5.1/nitrilase

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