Issue 21, 1992

Lipase-catalysed enantioselective acylation of N-protected or unprotected 2-aminoalkan-1-ols

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.

Article information

Article type
Paper

J. Chem. Soc., Perkin Trans. 1, 1992, 2885-2889

Lipase-catalysed enantioselective acylation of N-protected or unprotected 2-aminoalkan-1-ols

S. Fernández, R. Brieva, F. Rebolledo and V. Gotor, J. Chem. Soc., Perkin Trans. 1, 1992, 2885 DOI: 10.1039/P19920002885

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