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Title of article :
The lid is a structural and functional determinant of lipase activity and selectivity
Author/Authors :
Secundo، نويسنده , , Francesco and Carrea، نويسنده , , Giacomo and Tarabiono، نويسنده , , Chiara and Gatti-Lafranconi، نويسنده , , Pietro and Brocca، نويسنده , , Stefania and Lotti، نويسنده , , Marina and Jaeger، نويسنده , , Karl-Erich and Puls، نويسنده , , Michael and Eggert، نويسنده , , Thorsten، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
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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.
Keywords :
Bacillus subtilis lipase A , Pseudomonas fragi lipase , Specificity , Temperature stability , Candida rugosa lipase isoform 1 , Enantioselectivity , site-directed mutagenesis , domain swapping
Journal title :
Journal of Molecular Catalysis B Enzymatic
Journal title :
Journal of Molecular Catalysis B Enzymatic
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