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Titolo:
Molecular basis of lipase stereoselectivity
Autore:
Kovac, A; Scheib, H; Pleiss, J; Schmid, RD; Paltauf, F;
Indirizzi:
Graz Tech Univ, Dept Biochem & Food Chem, A-8010 Graz, Austria Graz Tech Univ Graz Austria A-8010 hem & Food Chem, A-8010 Graz, Austria Univ Stuttgart, Inst Tech Biochem, D-7000 Stuttgart, Germany Univ Stuttgart Stuttgart Germany D-7000 ochem, D-7000 Stuttgart, Germany
Titolo Testata:
EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY
fascicolo: 1, volume: 102, anno: 2000,
pagine: 61 - 77
SICI:
1438-7697(200001)102:1<61:MBOLS>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMICOLA-LANUGINOSA LIPASE; CANDIDA-RUGOSA LIPASE; X-RAY CRYSTALLOGRAPHY; MONOMOLECULAR FILM TECHNIQUE; RHIZOPUS-DELEMAR LIPASE; ACYL-CHAIN LENGTH; INTERFACIAL ACTIVATION; RHIZOMUCOR-MIEHEI; PANCREATIC LIPASE; SUBSTRATE-BINDING;
Keywords:
microbial lipases; site-directed mutagenesis; molecular modeling; enzyme-inhibitor complexes; synthetic substrates;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
104
Recensione:
Indirizzi per estratti:
Indirizzo: Paltauf, F Graz Tech Univ, Dept Biochem & Food Chem, Petersgasse 12-2, A-8010 Graz, Austria Graz Tech Univ Petersgasse 12-2 Graz Austria A-8010 z, Austria
Citazione:
A. Kovac et al., "Molecular basis of lipase stereoselectivity", EUR J LIPID, 102(1), 2000, pp. 61-77

Abstract

Lipases exhibit specific catalytic properties that make them attractive tobiotechnological applications. Most important are the broad substrate specificity and the regio- and stereoselectivity of lipases. Despite mechanistic and structural similarities lipases differ significantly with respect to stereoselectivity toward natural and synthetic substrates. Models developedto describe and predict stereoselectivity toward certain types of synthetic substrates, e.g., secondary alcohols cannot be applied to natural acylglycerols, that are hydrolyzed by several animal and microbial lipases in a regioselective or stereoselective manner. Therefore, computer-aided molecularmodeling studies were used in order to predict the stereopreference of lipases toward triradylglycerols. Lipase variants with modified stereoselectivity properties toward triacylglycerols were engineered by re-designing the recombinant enzyme. To understand the interactions governing lipase stereoselectivity towards natural substrates, knowledge of the structure of enzyme-substrate complexes at the atomic level is essential. Such information canbe obtained by X-ray or NMR analysis of covalent enzyme-inhibitor complexes. The crystal structures of enzymes complexed with triacylglycerol analog inhibitors allowed the identification of distinct binding sites for the three hydrophobic chains of the inhibitor.

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Documento generato il 04/12/20 alle ore 02:31:55