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Titolo:
Computer simulations of enantioselective ester hydrolyses catalyzed by Pseudomonas cepacia lipase
Autore:
Tafi, A; van Almsick, A; Corelli, F; Crusco, M; Laumen, KE; Schneider, MP; Botta, M;
Indirizzi:
Univ Siena, Dipartimento Farmacochim Tecnol, I-53100 Siena, Italy Univ Siena Siena Italy I-53100 Farmacochim Tecnol, I-53100 Siena, Italy Berg Univ Gesamthsch Wuppertal, FB Organ Chem 9, D-42097 Wuppertal, Germany Berg Univ Gesamthsch Wuppertal Wuppertal Germany D-42097 pertal, Germany
Titolo Testata:
JOURNAL OF ORGANIC CHEMISTRY
fascicolo: 12, volume: 65, anno: 2000,
pagine: 3659 - 3665
SICI:
0022-3263(20000616)65:12<3659:CSOEEH>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACTIVE-SITE MODEL; PURE SECONDARY ALCOHOLS; CANDIDA-RUGOSA LIPASE; ORGANIC-SYNTHESIS; PANCREATIC LIPASE; 2-ARYLPROPIONIC ESTERS; INTERFACIAL ACTIVATION; SUBSTRATE-SPECIFICITY; ENZYMATIC PREPARATION; STRUCTURAL BASIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Corelli, F Univ Siena, Dipartimento Farmacochim Tecnol, Via Aldo Moro, I-53100 Siena,Italy Univ Siena Via Aldo Moro Siena Italy I-53100 53100 Siena,Italy
Citazione:
A. Tafi et al., "Computer simulations of enantioselective ester hydrolyses catalyzed by Pseudomonas cepacia lipase", J ORG CHEM, 65(12), 2000, pp. 3659-3665

Abstract

On the basis of the X-ray crystal structure of the lipase from Pseudomonascepacia (PcL)-an enzyme representative for a whole family of Pseudomonas lipases (lipase PS, SAM-2, AK 10, and others with a high degree of homology 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 aromatic alcohols. The major goal of this project was the development of a binding model for PcL which is able to rationalize the experimental findings to predict "a priori" the enantioselective behavior of PcL toward a wider range of substrates. A two-step modeling procedure, namely, docking experiments 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 experiments) 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 enzymatic hydrolysis reaction, both the enantioselectivity and tolerance of the enzyme were then explained through the study of thetetrahedral intermediates, in turn constructed from the calculated dockinggeometries of 1a-12a.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 13:20:10