Mezzetti, A Schrag, JD Cheong, CS Kazlauskas, RJ 2024-01-21T05:12:12Z 2024-01-21T05:12:12Z 2021-09-01 2005-04 1074-5521 https://pubs.kist.re.kr/handle/201004/136622 Synthetic chemists often exploit the high enantioselectivity of lipases to prepare pure enantiomers of primary alcohols, but the molecular basis for this enantioselectivity is unknown. The crystal structures of two phosphonate transition-state analogs bound to Burkholderia cepacia lipase reveal this molecular basis for a typical primary alcohol: 2-methyl-3-phenyl-1-propanol. The enantiomeric alcohol moieties adopt surprisingly similar orientations, with only subtle differences that make it difficult to predict how to alter enantioselectivity. These structures, along with a survey of previous structures of enzyme bound enantiomers, reveal that binding of enantiomers does not involve an exchange of two substituent positions as most researchers assumed. Instead, the enantiomers adopt mirror-image packing, where three of the four substituents at the stereocenter lie in similar positions. The fourth substituent, hydrogen, points in opposite directions. English CELL PRESS PSEUDOMONAS-CEPACIA CRYSTAL-STRUCTURES STRUCTURAL-ANALYSIS PRIMARY ALCOHOLS BINDING MODES RESOLUTION HYDROLYSIS COMPLEXES CARBOXYPEPTIDASE STEREOCHEMISTRY Mirror-image packing in enantiomer discrimination: Molecular basis for the enantioselectivity of B-cepacia lipase toward 2-methyl-3-phenyl-1-propanol Article 10.1016/j.chembiol.2005.01.016 1 CHEMISTRY & BIOLOGY, v.12, no.4, pp.427 - 437 CHEMISTRY & BIOLOGY 12 4 427 437 scie scopus 000229065700007 2-s2.0-17844410348 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article PSEUDOMONAS-CEPACIA CRYSTAL-STRUCTURES STRUCTURAL-ANALYSIS PRIMARY ALCOHOLS BINDING MODES RESOLUTION HYDROLYSIS COMPLEXES CARBOXYPEPTIDASE STEREOCHEMISTRY Mirrage image Lipase Burkholderia cepacia Hydrogen bond Molecular modelling Enantiomer Enantioselectivity