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
Citations
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The molecular reaction vessels for a transesterification process created by molecular imprinting technique.
Zihui Meng,Zihui Meng,Koji Sode +2 more
TL;DR: A polymeric catalyst was synthesized by co‐polymerizing 4(5)‐vinylimidazole and itaconic acid with trimethylpropanol trimethacrylate micro spheres with p‐nitrophenyl acetate as template, and molecular imprinting process enhanced the νmax of the Polymeric catalyst 3‐fold.
Properties of hydrogel-entrapped lipase of thermophilic Pseudomonas aeruginosa BTS-2
TL;DR: Pseudomonas aeruginosa BTS-2 produced lipase optimally on a mineral based (MB) broth, supplemented with 1% (v/v) cottonseed oil as sole carbon source, after incubation at 56°C for 48 h.
Journal ArticleDOI
Characterization of ML-005, a Novel Metaproteomics-Derived Esterase.
TL;DR: ML-005 exhibited lipolytic activity toward short-chained substrates with the preferred substrate being p-nitrophenyl-butyrate, suggesting that ML-005 is an esterase, but remains stable in the presence of a range of metal ions, but addition of Cu2+ significantly reduces its relative activity.
Journal ArticleDOI
Interesterification reactions catalyzed by a lipase immobilized on a hydrophobic support.
TL;DR: Bacterial lipase from Pseudomonas cepacia immobilized on a hydrophobic support was used to bring about the interesterification reactions of the triglycerides of olive oil with octanoic acid, resulting in both faster initial rates of interesterization and eventually, as the mixture approached equilibrium, a higher fraction of octanoi acid residues in the glycerides of Olive oil.
Journal ArticleDOI
Investigation of the interaction of DAD1-LIKE LIPASE 3 (DALL3) with Selenium Binding Protein 1 (SBP1) in Arabidopsis thaliana.
Irene Dervisi,Chrysanthi Valassakis,Adamantia Agalou,Nikolaos Papandreou,Varvara Podia,Kosmas Haralampidis,Vassiliki A. Iconomidou,Vassili N. Kouvelis,Herman P. Spaink,Andreas Roussis +9 more
TL;DR: This work has studied AtDALL3 as an interacting partner of the Arabidopsis Selenium Binding Protein 1 (SBP1) and confirmed by yeast two hybrid assays the physical interaction of DALL3 with SBP1 and defined a minimal SBp1 fragment that Dall3 binds to.
References
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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.