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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Amino acid modified chitosan beads: Improved polymer supports for immobilization of lipase from Candida rugosa
TL;DR: In this paper, Amino acid modified chitosan beads (CBs) were used for the immobilization of lipases from Candida rugosa, where the beads were analyzed by elemental analysis and solid state NMR with coupling yields of the amino acids ranging from 15 to 60%.
Journal ArticleDOI
Improved production of a recombinant Rhizomucor miehei lipase expressed in Pichia pastoris and its application for conversion of microalgae oil to biodiesel
TL;DR: Improve the enzyme properties of RML in order to apply it for the conversion of microalgae oil to biofuel and demonstrate signal peptide optimization in the expression plasmid, addition of the gene propeptide, and proper gene dosage significantly increased RML expression level and enhanced the enzymatic properties.
Journal ArticleDOI
Chlorophyllase as a serine hydrolase: Identification of a putative catalytic triad
Tohru Tsuchiya,Takuo Suzuki,Takafumi Yamada,Hiroshi Shimada,Tatsuru Masuda,Hiroyuki Ohta,Ken-ichiro Takamiya +6 more
TL;DR: Results indicate that Chlase is a serine hydrolase and, by analogy with a plausible catalytic mechanism of serine Hydrolases, a mechanism for hydrolysis catalyzed by Chlases is proposed.
Journal ArticleDOI
Substrate specificity and kinetic properties of enzymes belonging to the hormone-sensitive lipase family: comparison with non-lipolytic and lipolytic carboxylesterases.
Henri Chahinian,Yassine Ben Ali,Abdelkarim Abousalham,Stefan Petry,Luigi Mandrich,Guiseppe Manco,Stéphane Canaan,Louis Sarda +7 more
TL;DR: Results indicate that human HSL, together with other lipolytic carboxylesterases, are active on short chain esters and hydrolyze water insoluble trioctanoin, vinyl laurate and olive oil, whereas the action of EST2, AFEST, protein RV1399C and non-lipolyticCarboxylesTERases is restricted to solutions of short chain substrates.
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.