Regioselective Acylation of Nucleosides Catalyzed by Candida Antarctica Lipase B: Enzyme Substrate Recognition

• Published in: European Journal of Organic Chemistry
• Main Authors: Li, Ning, Zong, Min‐Hua, Ma, Ding
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 2008
• Subjects: Organic Chemistry; Physical and Theoretical Chemistry; Antarc*; Antarctica
• Online Access: http://dx.doi.org/10.1002/ejoc.200800780; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fejoc.200800780; https://onlinelibrary.wiley.com/doi/full/10.1002/ejoc.200800780

Abstract The substrate recognition of Candida antarctica lipase B (CAL‐B) in the acylation of nucleosides was revealed through rational substrate engineering for the first time. CAL‐B displayed lower activities and excellent 5′‐regioselectivities (94 to >99 %) in the acylation of ribonucleosides 1f – 1j as compared to those in the acylation of 2′‐deoxynucleosides 1a – 1e . The excellent regioselectivities might be attributed to the favorable steric hindrance of the 2′‐hydroxy group present in ribonucleosides 1f – 1j , which destabilizes the conformation of the 3′‐acylation transition state in the acylation of 1f – 1j and thus reduces the amount of the minor regioisomer. The study of the acyl chain‐length specificity showed that CAL‐B was more specific toward short‐chain fatty acid vinyl esters, especially vinyl butyrate. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)