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Acylation of β‐Amino Esters and Hydrolysis of β‐Amido Esters: Candida antarctica Lipase A as a Chemoselective Deprotection Catalyst
Author(s) -
Mäenpää Harri,
Kanerva Liisa T.,
Liljeblad Arto
Publication year - 2016
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201501381
Subject(s) - candida antarctica , hydrolysis , acylation , chemistry , chemoselectivity , catalysis , amide , lipase , kinetic resolution , organic chemistry , peptide bond , amino acid , amino esters , enzyme , enantioselective synthesis , biochemistry
Abstract N‐Acylation by lipase A from Candida antarctica (CAL‐A) in ethyl butanoate was applied to the kinetic resolution of tert ‐butyl esters of 3‐amino‐3‐phenylpropanoic acid ( E >100), 3‐amino‐4‐methylpentanoic acid ( E >100) and 3‐aminobutanoic acid ( E =60) on 1.0–2.0 m scale. With the N‐acylated resolution products, the exceptional ability of CAL‐A to hydrolyse amides and bulky tert ‐butyl esters was then studied. In all N‐acylated tert ‐butyl esters, chemoselectivity favoured the amide bond cleavage. The tert ‐butyl ester bond was left intact with 3‐amino‐3‐phenylpropanoate, whereas with 3‐amino‐4‐methylpentanoate and 3‐aminobutanoate the CAL‐A‐catalysed hydrolysis of tert‐ butyl ester followed the amide hydrolysis.