Journal ArticleDOI
A serine protease triad forms the catalytic centre of a triacylglycerol lipase.
Leo Brady,Andrzej M. Brzozowski,Andrzej M. Brzozowski,Zygmunt S. Derewenda,Eleanor J. Dodson,Guy Dodson,S.P. Tolley,Johan P. Turkenburg,Lars Christiansen,Birgitte Huge-Jensen,Leif Norskov,Lars Thim,Ulrich Menge +12 more
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TLDR
The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.Abstract:
True lipases attach triacylglycerols and act at an oil-water interface; they constitute a ubiquitous group of enzymes catalysing a wide variety of reactions, many with industrial potential. But so far the three-dimensional structure has not been reported for any lipase. Here we report the X-ray structure of the Mucor miehei triglyceride lipase and describe the atomic model obtained at 3.1 A resolution and refined to 1.9 A resolution. It reveals a Ser..His..Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.read more
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Journal ArticleDOI
Immobilization of lipases by selective adsorption on hydrophobic supports.
Roberto Fernandez-Lafuente,Pilar Armisén,Pilar Sabuquillo,Gloria Fernández-Lorente,Jose M. Guisan +4 more
TL;DR: Different approaches for lipase immobilization mainly related to the further use of immobilized derivatives to carry out enantio and regioselective hydrolysis in high water-activity systems are reviewed.
Journal ArticleDOI
Converting Trypsin to Chymotrypsin: The Role of Surface Loops
TL;DR: This mutant enzyme is equivalent to Ch in its catalytic rate, but its substrate binding is impaired and it utilizes extended substrate binding to accelerate catalysis, and substrate discrimination occurs during the acylation step rather than in substrate binding.
Journal ArticleDOI
Lipase promiscuity and its biochemical applications
Manali Kapoor,Munishwar N. Gupta +1 more
TL;DR: This review attempts to recast the known information on specificity of lipases in the context of enzyme promiscuity and the beneficial consequences of this promiscuous behavior in biotechnology sectors are discussed.
Journal ArticleDOI
Bacterial dehalogenases: biochemistry, genetics, and biotechnological applications.
Susanne Fetzner,Franz Lingens +1 more
TL;DR: This review is a survey of bacterial dehalogenases that catalyze the cleavage of halogen substituents from haloaromatics, haloalkanes, h Haloalcohols, and h Haloalkanoic acids.
Journal ArticleDOI
Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
Jose M. Palomo,Gloria Muñoz,Gloria Fernández-Lorente,Cesar Mateo,Roberto Fernandez-Lafuente,Jose M. Guisan +5 more
TL;DR: It seems that the “open structure” of lipases, adsorbed on hydrophobic supports, is much more active and much more stable than the corresponding “closed” structure even when the closed structure is undergoing a very intense multipoint covalent attachment.
References
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Journal ArticleDOI
Human lipoprotein lipase complementary DNA sequence
TL;DR: Analysis of the sequence indicates that human lipoprotein lipase, hepaticlipase, and pancreatic lipase are members of a gene family that acts to hydrolyze triglycerides, providing free fatty acids for cells and affecting the maturation of circulating lipoproteins.