Enzymatic resolution of methyl (2E, 4R*,5S*)-4-(N-benzyl-N-methyl)amino-5-hydroxyhex-2-enoate

Autor:	Hiroyuki Akita, Miyuki Sato, Mikio Fujii, Machiko Ono
Rok vydání:	2011
Předmět:	chemistry.chemical_classification biology Resolution (mass spectrometry) Process Chemistry and Technology Bioengineering Optically active Biochemistry Catalysis Reaction product Acylation Enzyme chemistry biology.protein Organic chemistry Lipase Vicinal
Zdroj:	Journal of Molecular Catalysis B: Enzymatic. 69:21-26
ISSN:	1381-1177
Popis:	For the purpose of preparation of optically active aminoalcohol congeners possessing both hydroxyl- and dialkylamino-substituted vicinal chiral carbons, lipase-assisted acylation of methyl (2E,4R*,5S*)-4-(N-benzyl-N-methyl)amino-5-hydroxyhex-2-enoate (4) using CAL-B with vinyl hexanoate as an acyl donor was carried out to give (4S,5R)-hexenoate (7) (44%, 99.2% ee) as the reaction product and (4R,5S)-alcohol (4) (46%, 98.2% ee) as the unreacted starting material. The E-value of the present lipase-assisted resolution was estimated to be more than 1000. Thus obtained acylated product was successfully converted into methyl β-d-vicenisaminide (12).
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::91f76665605e166b1562cd1309c15b3e https://doi.org/10.1016/j.molcatb.2010.12.005 Zobrazit plný text záznamu Full Text from ScienceDirect