Complex of Burkholderia cepacia lipase with transition state analogue of 1‐phenoxy‐2‐acetoxybutane

Abstract

In a series of four racemic phenoxyalkyl‐alkyl carbinols, 1‐phenoxy‐2‐hydroxybutane ( 1 ) is enantioselectively acetylated by Burkholderia cepacia (formerly Pseudomonas cepacia ) lipase with an E value ≥ 200, whereas for the other three racemates E was found to be ≤ 4. To explain the high preference of B. cepacia lipase for ( R )‐(+)‐ 1 , a precursor of its transition state analogue with a tetrahedral P‐atom, ( R P ,S P ) ‐O‐ (2 R )‐(1‐phenoxybut‐2‐yl)methylphosphonic acid chloride was prepared and crystallized in complex with B. cepacia lipase. The X‐ray structure of the complex was determined, allowing to compare the conformation of the inhibitor with results of molecular modelling.