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Autor(en): Henke, Erik
Bornscheuer, Uwe Theo
Schmid, Rolf D.
Pleiss, Jürgen
Titel: The molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases
Erscheinungsdatum: 2003
Dokumentart: Preprint
Erschienen in: ChemBioChem 4 (2003), S. 485-493. URL http://dx.doi.org./10.1002/cbic.200200518
URI: http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26732
http://elib.uni-stuttgart.de/handle/11682/848
http://dx.doi.org/10.18419/opus-831
Zusammenfassung: Carboxylesterases containing the sequence motif GGGX catalyze hydrolysis of esters of chiral tertiary alcohols, albeit at only low to moderate enantioselectivity towards three model substrates (linalyl acetate, methyl-1-pentin-1-yl acetate, 2-phenyl-3-butin-2-yl acetate). In order to understand the molecular mechanism of enantiorecognition and to improve enantioselectivity towards this interesting substrate class, the interaction of both enantiomers with the substrate binding sites of acetylcholinesterases and p-nitrobenzyl esterase from Bacillus subtilis was modeled and correlated to experimental enantioselectivity. For all substrate-enzyme pairs, enantiopreference and ranking by enantioselectivity could be predicted by the model. In p-nitrobenzyl esterase, one of the key residues in determining enantioselectivity was G105: exchange of this residue by alanine led to a six-fold increase of enantioselectivity (E=19) towards 2-phenyl-3-butin-2-yl acetate. However, the effect of this mutation is personalized: towards the substrate linalyl acetate, the same mutant had a reversed enantiopreference. Thus, depending on the substrate structure, the same mutant had either increased enantioselectivity or opposite enantiopreference compared to wild type enzyme.
Enthalten in den Sammlungen:03 Fakultät Chemie

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