http://www.cnr.it/ontology/cnr/individuo/prodotto/ID17429

The lid is a structural and functional determinant of lipase activity and selectivity (Articolo in rivista)

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The lid is a structural and functional determinant of lipase activity and selectivity (Articolo in rivista) (literal)

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Francesco Secundo; Giacomo Carrea; Chiara Tarabiono; Pietro Gatti-Lafranconi; Stefania Brocca; Marina Lotti; Karl-Erich Jaeger; Michael Puls; Thorsten Eggert. (2006)
The lid is a structural and functional determinant of lipase activity and selectivity
in Journal of molecular catalysis. B, Enzymatic (Online); ELSEVIER SCIENCE BV, PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS, AMSTERDAM (Paesi Bassi)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Francesco Secundo; Giacomo Carrea; Chiara Tarabiono; Pietro Gatti-Lafranconi; Stefania Brocca; Marina Lotti; Karl-Erich Jaeger; Michael Puls; Thorsten Eggert. (literal)

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CNR, Ist Chim Riconoscimento Mol, I-20131 Milan, Italy Univ Milano Bicocca, Dipartimento Biotecnol & Biosci, I-20126 Milan, Italy Univ Dusseldorf, Inst Mol Enzymtechnol, Forschungszentrum Julich, D-52426 Julich, Germany (literal)

Titolo

The lid is a structural and functional determinant of lipase activity and selectivity (literal)

Abstract

In several lipases access to the enzyme active site is regulated by the position of a mobile structure named the lid. The role of this region in modulating lipase function is reviewed in this paper analysing the results obtained with three different recombinant lipases modified in the lid sequence: Candida rugosa lipase isoform 1 (CRL1), Pseudomonas fragi lipase (PFL) and Bacillus subtilis lipase A (BSLA). A CRL chimera enzyme obtained by replacing its lid with that of another C. rugosa lipase isoform (CRL1LID3) was found to be affected in both activity and enantioselectivity in organic solvent. Variants of the PFL protein in which three polar lid residues were replaced with amino acids strictly conserved in homologous lipases displayed altered chain length preference profile and increased thermostability. On the other hand, insertion of lid structures from structurally homologous enzymes into BSLA, a lipase that naturally does not possess such a lid structure, caused a reduction in the enzyme activity and an altered substrate specificity. These results strongly support the concept that the lid plays an important role in modulating not only activity but also specifity, enantioselectivity and stability of lipase enzymes. (literal)

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