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http://dx.doi.org/10.18419/opus-831
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DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Henke, Erik | de |
dc.contributor.author | Bornscheuer, Uwe Theo | de |
dc.contributor.author | Schmid, Rolf D. | de |
dc.contributor.author | Pleiss, Jürgen | de |
dc.date.accessioned | 2006-06-01 | de |
dc.date.accessioned | 2016-03-31T07:46:44Z | - |
dc.date.available | 2006-06-01 | de |
dc.date.available | 2016-03-31T07:46:44Z | - |
dc.date.issued | 2003 | de |
dc.identifier.other | 262546825 | de |
dc.identifier.uri | http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-26732 | de |
dc.identifier.uri | http://elib.uni-stuttgart.de/handle/11682/848 | - |
dc.identifier.uri | http://dx.doi.org/10.18419/opus-831 | - |
dc.description.abstract | 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. | en |
dc.language.iso | en | de |
dc.rights | info:eu-repo/semantics/openAccess | de |
dc.subject.classification | Bioinformatik , Molekulare Bioinformatik , Proteindesign , Carboxylesterase | de |
dc.subject.ddc | 540 | de |
dc.subject.other | enantioselectivity , enzyme catalysis , molecular modeling , protein design , tertiary alcohols | en |
dc.title | The molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases | en |
dc.type | preprint | de |
dc.date.updated | 2015-12-10 | de |
ubs.fakultaet | Fakultät Chemie | de |
ubs.fakultaet | Fakultätsübergreifend / Sonstige Einrichtung | de |
ubs.institut | Institut für Technische Biochemie | de |
ubs.institut | Sonstige Einrichtung | de |
ubs.opusid | 2673 | de |
ubs.publikation.source | ChemBioChem 4 (2003), S. 485-493. URL http://dx.doi.org./10.1002/cbic.200200518 | de |
ubs.publikation.typ | Preprint | de |
Enthalten in den Sammlungen: | 03 Fakultät Chemie |
Dateien zu dieser Ressource:
Datei | Beschreibung | Größe | Format | |
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Henke_2003.pdf | 136,33 kB | Adobe PDF | Öffnen/Anzeigen |
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