Literature DB >> 18491860

Formation of enantiopure 5-substituted oxazolidinones through enzyme-catalysed kinetic resolution of epoxides.

Maja Majerić Elenkov1, Lixia Tang, Auke Meetsma, Bernhard Hauer, Dick B Janssen.   

Abstract

Halohydrin dehalogenase from Agrobacterium radiobacter catalyzed the enantioselective ring opening of terminal epoxides with cyanate as a nucleophile, yielding 5-substituted oxazolidinones in high yields and with high enantiopurity (69-98% ee). This is the first example of the biocatalytic conversion of a range of epoxides to the corresponding oxazolidinones.

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Year:  2008        PMID: 18491860     DOI: 10.1021/ol800698t

Source DB:  PubMed          Journal:  Org Lett        ISSN: 1523-7052            Impact factor:   6.005


  3 in total

1.  Highly α-position regioselective ring-opening of epoxides catalyzed by halohydrin dehalogenase from Ilumatobacter coccineus: a biocatalytic approach to 2-azido-2-aryl-1-ols.

Authors:  Miao An; Wanyi Liu; Xiaoying Zhou; Ran Ma; Huihui Wang; Baodong Cui; Wenyong Han; Nanwei Wan; Yongzheng Chen
Journal:  RSC Adv       Date:  2019-05-24       Impact factor: 3.361

2.  Enhancing the biocatalytic manufacture of the key intermediate of atorvastatin by focused directed evolution of halohydrin dehalogenase.

Authors:  Yu Luo; Yangzi Chen; Hongmin Ma; ZhenHua Tian; Yeqi Zhang; Jian Zhang
Journal:  Sci Rep       Date:  2017-02-06       Impact factor: 4.379

Review 3.  Recent advances on halohydrin dehalogenases-from enzyme identification to novel biocatalytic applications.

Authors:  Anett Schallmey; Marcus Schallmey
Journal:  Appl Microbiol Biotechnol       Date:  2016-08-08       Impact factor: 4.813

  3 in total

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