Journal
ADVANCED SYNTHESIS & CATALYSIS
Volume 349, Issue 8-9, Pages 1393-1398Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/adsc.200600641
Keywords
enantioselectivity; enzyme catalysis; hydrolases; steric hindrance; tertiary alcohols
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The kinetic resolution of a series of acetates of arylaliphatic tertiary alcohols was studied using recombinant esterase variants from Bacillus subtilis (BS2) expressed in E. coli. Highest enantioselectivities (E > 100) were achieved in the synthesis of 1,1,1-trifluoro-2-phenylbut-3-yn-2-ol and three para-substituted analogues using BS2 mutant G105A. With mutant E188D only two compounds were converted with E > 100. For a thiophene analogue or compounds with small variations in the aliphatic chain substantially lower conversions and/or enantioselectivity were observed, which also varied with the BS2 variant used. Thus, small changes in the substrate structure and point mutations in the esterase had a remarkable influence on both activity and enantioselectivity.
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