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
The structure of Staphylococcus aureus epidermolytic toxin A, an atypic serine protease, at 1.7 Å resolution
Jean Cavarelli,Gilles Prévost,William Bourguet,Luc Moulinier,Bernard Chevrier,Bénédicte Delagoutte,Alexandrine Bilwes,Lionel Mourey,Samer Rifai,Y Piémont,Dino Moras +10 more
TL;DR: Despite very low sequence homology between ETA and other trypsin-like serine proteases, the ETA crystal structure, together with biochemical data and site-directed mutagenesis studies, strongly confirms the classification of ETA in the Glu-endopeptidase family.
Journal ArticleDOI
Purification, immobilization, and stabilization of a lipase from Bacillus thermocatenulatus by interfacial adsorption on hydrophobic supports.
Jose M. Palomo,Rosa L. Segura,Gloria Fernández-Lorente,María A. Pernas,María L. Rúa,Jose M. Guisan,Roberto Fernandez-Lafuente +6 more
TL;DR: A lipase from Bacillus thermocatenulatus cloned in E. coli has been purified using a very simple method: interfacial activation on a hydrophobic support followed by desorption with Triton.
Journal ArticleDOI
Cloning, expression and characterization of a cDNA encoding a lipase from Rhizopus delemar.
TL;DR: It is concluded that the LIP cDNA is an essentially full-length analogue of the lipase-encoding gene of Rp.
Journal ArticleDOI
Purification, molecular cloning, and expression of lipase from Pseudomonas aeruginosa.
Mikiko Chihara-Siomi,Kazuhiro Yoshikawa,Noriko Oshima-Hirayama,Yamamoto Kazumi,Yukihiro Sogabe,Takuji Nakatani,Takaaki Nishioka,Jun'ichi Oda +7 more
TL;DR: The results of alignment of the amino acid sequences of five lipases from Pseudomonas species considered together with the published crystal structure studied with human pancreatic lipase showed that Ser82, His251, and Asp209 were catalytic residues and that a surface loop from residues 172 to 204 was responsible for the substrate specificity.
Journal ArticleDOI
A putative lipase gene EXTRA GLUME1 regulates both empty-glume fate and spikelet development in rice
Haoge Li,Dawei Xue,Dawei Xue,Zhenyu Gao,Meixian Yan,Wenying Xu,Zhuo Xing,Danian Huang,Danian Huang,Qian Qian,Qian Qian,Yongbiao Xue +11 more
TL;DR: The cloning of the rice EXTRA GLUME1 gene reveals a novel pathway that regulates rice empty-glume fate and spikelet development and is probably responsible for the pleiotropic floral defects in eg1.
References
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Journal ArticleDOI
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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.