Lipase-catalysed enantioselective acylation of N-protected or unprotected 2-aminoalkan-1-ols
- 1 January 1992
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Perkin Transactions 1
- No. 21,p. 2885-2889
- https://doi.org/10.1039/p19920002885
Abstract
Porcine pancreatic lipase (PPL) catalysed the acylation of 2-aminoalkan-1-ols; the enantiospecificity depends on the starting amino alcohol. The catalytic activity of the enzyme was markedly improved when the benzyl carbamate derivatives were used as substrates; in general, the enzyme displayed a high enantiospecificity.Keywords
This publication has 12 references indexed in Scilit:
- Enzyme assisted preparation of enantiomerically pure β-adrenergic blockers II. Building blocks of high optical purity and their synthetic conversionTetrahedron: Asymmetry, 1992
- Enzymatic aminolysis and transamidation reactionsTetrahedron, 1991
- Esterolytic and Lipolytic Enzymes in Organic SynthesisSynthesis, 1991
- Oxime Esters as Acylating Agents in the Aminolysis Reaction. A Simple and Chemoselective Method for the Preparation of Amides from Amino AlcoholsSynthesis, 1991
- Stereoselective syntheses of ephedrine and related 2-aminoalcohols of high optical purity from protected cyanohydrinsTetrahedron Letters, 1990
- β-Amino alcohols from amino acids: Chelation control via schiff bases.Tetrahedron Letters, 1990
- N4-isopropyl-N-methyl formamidine, a reagent for the synthesis of bioactive amino-alcohols.Tetrahedron Letters, 1990
- Enantioselective acylation of amino alcohols by porcine pancreatic lipaseJournal of the Chemical Society, Chemical Communications, 1988
- Lipase-catalyzed resolution of chiral 2-amino 1-alcoholsThe Journal of Organic Chemistry, 1987
- Preparation of protected amino aldehydesThe Journal of Organic Chemistry, 1981