Reference : Study of thermomyces ianuginosa lipase in the presence of tributyrylglycerol and water
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/16005
Study of thermomyces ianuginosa lipase in the presence of tributyrylglycerol and water
English
Santini, Sébastien [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Centre de Biophysique Moléculaire Numérique > >]
Crowet, Jean-Marc mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Thomas, Annick mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Paquot, Michel [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Unité de Chimie Biologique Industrielle > >]
Vandenbol, Micheline mailto [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Unité de Biologie animale et microbienne > >]
Thonart, Philippe mailto [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech - Biochimie et microbiologie industrielles > > >]
Wathelet, Jean-Paul mailto [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Unité de Chimie Générale Organique > >]
Blecker, Christophe [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Unité de Technologies des Industries Agro-Alimentaires > >]
Lognay, Georges mailto [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Unité de Chimie Analytique > >]
Brasseur, Robert mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Lins, Laurence mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Charloteaux, Benoît [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Jun-2009
Biophysical Journal
Biophysical Society
96
12
4814-4825
Yes (verified by ORBi)
International
0006-3495
1542-0086
Bethesda
MD
[en] Thermomyces lanuginosa Lipase ; Tributyrylglycerol ; Water
[en] The Thermomyces lanuginosa lipase has been extensively studied in industrial and biotechnological research because of its potential for triacylglycerol transformation. This protein is known to catalyze both hydrolysis at high water contents and transesterification in quasi-anhydrous conditions. Here, we investigated the Thermomyces lanuginosa lipase structure in
solution in the presence of a tributyrin aggregate using 30 ns molecular-dynamics simulations. The water content of the active-site groove was modified between the runs to focus on the protein-water molecule interactions and their implications for protein structure and protein-lipid interactions. The simulations confirmed the high plasticity of the lid fragment and showed
that lipid molecules also bind to a secondary pocket beside the lid. Together, these results strongly suggest that the lid plays a role in the anchoring of the protein to the aggregate. The simulations also revealed the existence of a polar channel that connects the active-site groove to the outside solvent. At the inner extremity of this channel, a tyrosine makes hydrogen bonds
with residues interacting with the catalytic triad. This system could function as a pipe (polar channel) controlled by a valve (the tyrosine) that could regulate the water content of the active site.
Researchers ; Professionals
http://hdl.handle.net/2268/16005
10.1016/j.bpj.2009.03.040
http://www.sciencedirect.com/science?_ob=PublicationURL&_cdi=56421&_pubType=J&_acct=C000026700&_version=1&_urlVersion=0&_userid=532081&md5=150bf8ef8f3fc7217017e3ca06ecbe42&jchunk=96#96

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