Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane, Biocatalytic, structural and modelling study. (CROSBI ID 86969)
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Podaci o odgovornosti
Luić, Marija ; Tomić, Sanja ; Leščić, Ivana ; Ljubović, Edina ; Šepac, Dragan ; Šunjić, Vitomir ; Vitale, Ljubinka ; Saenger, Wolfram ; Kojić-Prodić, Biserka
engleski
Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane, Biocatalytic, structural and modelling study.
In a series of four racemic phenoxyalkyl-alkyl carbinols, 1-phenoxy-2-hydroxy butane (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, (RP,SP)-methyl-O-(2R)-1-phenoxybut-2-yl) phosphonic acid chloride was prepared and crystallised 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.
Burkholderia cepacia lipase; Pseudomonas cepacia lipase; racemic sec alcohols; transition state (TS) analogue; crystal structure; molecular modelling
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