Enzymatic resolution of racemic glycals: an application of the wong acylation method

David B. Berkowitz; Samuel J. Danishefsky

doi:10.1016/0040-4039(91)80067-G

Enzymatic resolution of racemic glycals: an application of the wong acylation method

David B. Berkowitz, Samuel J. Danishefsky

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Kinetic resolution of racemic, fully synthetic, artificial glycals bearing a free hydroxyl group at C₃ was accomplished through the more rapid acylation of the "D"-antipode with vinyl acetate as acyl donor and Lipase PS-30 from Pseudomonas cepacia as catalyst.

Original language	English (US)
Pages (from-to)	5497-5500
Number of pages	4
Journal	Tetrahedron Letters
Volume	32
Issue number	40
DOIs	https://doi.org/10.1016/0040-4039(91)80067-G
State	Published - Sep 30 1991
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Drug Discovery
Organic Chemistry

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title = "Enzymatic resolution of racemic glycals: an application of the wong acylation method",

abstract = "Kinetic resolution of racemic, fully synthetic, artificial glycals bearing a free hydroxyl group at C3 was accomplished through the more rapid acylation of the {"}D{"}-antipode with vinyl acetate as acyl donor and Lipase PS-30 from Pseudomonas cepacia as catalyst.",

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