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Enzyme‐Catalyzed Nucleophilic Ring Opening of Epoxides for the Preparation of Enantiopure Tertiary Alcohols
Author(s) -
Elenkov Maja Majerić,
Hoeffken H. Wolfgang,
Tang Lixia,
Hauer Bernhard,
Janssen Dick B.
Publication year - 2007
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200700146
Subject(s) - enantiopure drug , chemistry , kinetic resolution , nucleophile , azide , biocatalysis , ring (chemistry) , tertiary alcohols , catalysis , cyanide , nucleophilic substitution , organic chemistry , enzyme , substrate (aquarium) , combinatorial chemistry , enantioselective synthesis , reaction mechanism , oceanography , geology
The halohydrin dehalogenase from Agrobacterium radiobacter AD1 (HheC) catalyzes nucleophilic ring opening of epoxides with cyanide and azide. In the case of 2,2‐disubstituted epoxides, this reaction proceeds with excellent enantioselectivity (E values up to>200), which gives, by kinetic resolution, access to various enantiopure epoxides and β‐substituted tertiary alcohols ( ee up to 99 %). Since the enzyme has a broad substrate range and because these tertiary alcohols are difficult to prepare in other ways, HheC is an attractive biocatalyst for the production of β‐cyano and β‐azido tertiary alcohols.