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Synfacts 2007(8): 0876-0876  
DOI: 10.1055/s-2007-968757
Organo- and Biocatalysis
© Georg Thieme Verlag Stuttgart · New York

Enzyme Catalysis towards Optically Pure β-Hydroxy Nitriles

Contributor(s): Benjamin List, Corinna Reisinger
D. Zhu, H. Ankati, C. Mukherjee, Y. Yang, E. R. Biehl, L. Hua*
Southern Methodist University, Dallas, USA
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Publication History

Publication Date:
24 July 2007 (online)

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Significance

A carbonyl reductase from Candida magnoliae (CMCR) was found to catalyze the highly chemo- and enantioselective reduction of a range of aromatic β-keto nitriles 1. NADPH is used as cofactor together with a d-glucose and d-glucose dehydrogenase (GDH) system for cofactor regeneration. (R)-β-hydroxy nitriles 2 have been further converted into the corresponding (R)-β-hydroxycarboxylic acids 3 via a nitrilase (NIT6803)-catalyzed hydrolysis proceeding under neutral conditions. Notably, the aliphatic cyano group in substrate 4 could be selectively hydrolyzed by changing to nitrilase bll6402 from Bradyrhizobium japonicum strain USDA110.