Current Organic Chemistry

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Stereoselective Enzymatic Acylations (Transesterifications)

Author(s): Robert Chenevert, Nicholas Pelchat, Frederic Jacques.

Abstract:

Hydrolytic enzymes such as lipases and esterases are the most frequently used biocatalysts in organic synthesis. They have as their natural function, the hydrolysis of ester substrates in water. These enzymes are also active in organic solvents of low polarity, and the main advantage of reactions in hydrophobic media is the ability to carry out esterifications instead of hydrolyses. The hydrolase-catalyzed formation of esters from alcohols and ester acyl donors (transesterification) is a reversible reaction. The use of activated esters as acyl donors shifts the equilibrium constant in favor of the product. Several activated esters have been developed, but the most useful acyl donors are enol esters such as vinyl acetate. After providing general background information, this review describes recent applications of stereoselective enzymatic acylations (transesterifications) in the preparation of chiral non-racemic compounds. The main focus is on the potential use of this process in the synthesis of biologically active compounds and natural products.

Keywords: resonance energy, Acyl Donors, sulfation, Enantioconvergent synthesis, cross-linked enzyme crystal (CLEC), cytoxazone

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Article Details

VOLUME: 10
ISSUE: 10
Page: [1067 - 1094]
Pages: 28
DOI: 10.2174/138527206777698093
Price: $58