Identification of MsrA homologues for the preparation of (R)-sulfoxides at high substrate concentrations. Issue 13 (12th March 2019)

• Record Type: Journal Article
• Authors: Yang, Jiawei; Wen, Yuanmei; Peng, Liaotian; Chen, Yu; Cheng, Xiaoling; Chen, Yongzheng
• Is Part Of: Organic & biomolecular chemistry. Volume 17:Issue 13(2019)
• Page Start: 3381
• Page End: 3388
• Publication Date: 2019-03-12
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c9ob00384c
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : An MsrA homologue with extremely high substrate tolerance and a wide substrate scope for the biocatalytic preparation of enantiopure sulfoxides. Abstract : Here we report a methionine sulfoxide reductase A (MsrA) homologue with extremely high substrate tolerance and a wide substrate scope for the biocatalytic preparation of enantiopure sulfoxides. This MsrA homologue which was obtained from Pseudomonas alcaliphila (named pa MsrA) showed good activity and enantioselectivity towards a series of aryl methyl/ethyl sulfoxides1a–1k, with electron-withdrawing or electron-donating substituents at the aromatic ring. Chiral sulfoxides in the R configuration were prepared with approximately 50% of yield and up to 99% enantiomeric excess through the asymmetric reductive resolution of racemic sulfoxide catalyzed by the recombinant pa MsrA protein. More importantly, kinetic resolution has been successfully accomplished with high enantioselectivity ( E > 200) at initial substrate concentrations up to 320 mM (approximately 45 g L −1 ), which represents a great improvement in the aspect of the substrate concentration for the biocatalytic preparation of chiral sulfoxides.