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
An Insight into the Active Site of Pseudomonas Fluorecens (P. cepacia) Lipase to Define the Stereochemical Demand for the Transesterification in Organic Solvents
TL;DR: The Pseudomonas fluorescens lipase-catalyzed transesterification of 2-methyl alkanols 1 and the 2-substituted oxiranemethanols 2 with vinyl acetate in organic solvents has been studied and the results discussed in terms of steric and electronic demand within the recently postulated models of the lipase active site.
Journal ArticleDOI
Purification and characterization of intracellular lipase from the polyunsaturated fatty acid-producing fungus Mortierella alliacea
Worapol Jermsuntiea,Tsunehiro Aki,Rieko Toyoura,Kazuhiro Iwashita,Seiji Kawamoto,Kazuhisa Ono +5 more
TL;DR: The results indicate that triacylglycerol may be formed via 2-monoacyl glycerol, and the highly stable M. alliacea lipase may be useful for the synthesis of structured lipids, particularly acylglycerols containing functional unsaturated fatty acids at the sn-2 position.
Journal ArticleDOI
Structure of hydrolases: lipases and cellulases
TL;DR: The structural characterization of the opening mechanism of the active site of lipases, as first described for Rhizomucor miehei lipase, has been extended to the pancreatic lipase-colipase system, and to the Geotrichum candidum/Candida rugosa lipases.
Journal ArticleDOI
Hydrolysis of fish oil by hyperactivated Rhizomucor miehei lipase immobilized by multipoint anion exchange.
Marco Filice,Marzia Marciello,Lorena Betancor,Alfonso V. Carrascosa,Jose M. Guisan,Gloria Fernández-Lorente +5 more
TL;DR: These new hyperactivated derivatives seem to be more suitable for hydrolysis of oils by RML immobilized inside porous supports, and are fairly stable against heat and organic cosolvents.
Journal ArticleDOI
Synthesis, self-assembly, and catalytic activity of histidine-based structured lipopeptides for hydrolysis reactions in water
TL;DR: In this article, a series of lipopeptides was designed to study their organocatalytic properties towards ester hydrolysis and the role of their self-assembled structures in catalysis.
References
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Journal ArticleDOI
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Book ChapterDOI
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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.