Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4476
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dc.contributor.authorTafi, Andreaen_us
dc.contributor.authorVan Almsick, Andreasen_us
dc.contributor.authorCorelli, Federicoen_us
dc.contributor.authorCrusco, Mariaen_us
dc.contributor.authorLaumen Kurt, E.en_us
dc.contributor.authorSchneider Manfred, P.en_us
dc.contributor.authorBotta, Maurizioen_us
dc.date.accessioned2021-03-30T14:44:18Z-
dc.date.available2021-03-30T14:44:18Z-
dc.date.issued2000-
dc.identifier.issn0022-3263en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/4476-
dc.description44549en_US
dc.description.abstractOn the basis of the X-ray crystal structure of the lipase from Pseudomonas cepacia (PcL), an enzyme representative for a whole family of Pseudomonas lipases (lipase PS, SAM-2, AK 10, and others with a high degree of homol. with PcL), a computational study was performed to rationalize both the enantioselectivity and substrate specificity (tolerance) displayed by this lipase in the enantioselective hydrolysis of racemic esters 1a-12a from various secondary arom. alcs. The major goal of this project was the development of a binding model for PcL which is able to rationalize the exptl. findings to predict a priori the enantioselective behavior of PcL toward a wider range of substrates. A two-step modeling procedure, namely, docking expts. followed by construction of tetrahedral intermediates, was used for the simulation of the involved enzyme-substrate recognition/hydrolysis processes. The study of the recognition process (docking expts.) led to unambiguous identification of the binding geometry for the two enantiomeric series of substrates, but did not suggest a definitive interpretation of the behavior of PcL. Taking into consideration the stereoelectronic requirements of the enzymic hydrolysis reaction, both the enantioselectivity and tolerance of the enzyme were then explained through the study of the tetrahedral intermediates, in turn constructed from the calcd. docking geometries of 1a-12a.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofJOURNAL OF ORGANIC CHEMISTRYen_US
dc.titleComputer Simulations of Enantioselective Ester Hydrolyses Catalyzed by Pseudomonas cepacia Lipaseen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/jo9919198en_US
dc.identifier.pmid10864749en_US
dc.identifier.scopus2-s2.0-0034674696en_US
dc.identifier.isiWOS:000087609100012en_US
dc.relation.volume65en_US
dc.relation.issue12en_US
dc.description.firstpage3659en_US
dc.description.lastpage3665en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0003-4308-3531-
crisitem.author.orcid0000-0002-5750-4504-
crisitem.author.orcid0000-0003-0456-6995-
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