ORBi: Santini Sébastien - Study of thermomyces ianuginosa lipase in the presence of tributyrylglycerol and water

Reference : Study of thermomyces ianuginosa lipase in the presence of tributyrylglycerol and water


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/16005

Title :	Study of thermomyces ianuginosa lipase in the presence of tributyrylglycerol and water
Language :	English
Author, co-author :	Santini, Sébastien [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Centre de Biophysique Moléculaire Numérique > >]
	Crowet, Jean-Marc [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
	Thomas, Annick [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 [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Unité de Biologie animale et microbienne > >]
	Thonart, Philippe [Université de Liège - ULg > Gembloux Agro-Bio Tech > Gembloux Agro-Bio Tech - Biochimie et microbiologie industrielles > > >]
	Wathelet, Jean-Paul [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 [Université de Liège - ULg > Faculté Universitaire des Sciences Agronomiques de Gembloux > Unité de Chimie Analytique > >]
	Brasseur, Robert [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
	Lins, Laurence [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. >]
Publication date :	Jun-2009
Journal title :	Biophysical Journal
Publisher :	Biophysical Society
Volume :	96
Issue/season :	12
Pages :	4814-4825
Audience :	International
ISSN :	0006-3495
e-ISSN :	1542-0086
City :	Bethesda
Country :	MD
Keywords :	[en] Thermomyces lanuginosa Lipase ; Tributyrylglycerol ; Water
Abstract :	[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.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/16005
DOI :	10.1016/j.bpj.2009.03.040
Other URL :	http://www.sciencedirect.com/science?_ob=PublicationURL&_cdi=56421&_pubType=J&_acct=C000026700&_version=1&_urlVersion=0&_userid=532081&md5=150bf8ef8f3fc7217017e3ca06ecbe42&jchunk=96#96

File(s) associated to this reference

Fulltext file(s):

	File	Commentary	Version	Size	Access
Restricted access	Study of Thermomyces lanuginosa Lipase.pdf		Author postprint	128.16 kB	Request copy

All documents in ORBi are protected by a user license.

Dspace v1.5