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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Modeling of solvent-dependent conformational transitions in Burkholderia cepacia lipase
TL;DR: Molecular dynamics simulations of a closed homology model and an open crystal structure of Burkholderia cepacia lipase in water and toluene were performed to investigate the influence of solvents on structure, dynamics, and the conformational transition of the lid.
Journal ArticleDOI
Identification of the active site serine of hormone‐sensitive lipase by site‐directed mutagenesis
Cecilia Holm,Richard C. Davis,Richard C. Davis,Torben Østerlund,Michael C. Schotz,Michael C. Schotz,Gudrun Fredrikson +6 more
TL;DR: Results suggest that Ser‐423 is the active site serine of hormone‐sensitive lipase, and substitution by several different amino acids resulted in the complete abolition of both lipase and esterase activity.
Journal ArticleDOI
Acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides, has phospholipase, lysophospholipase, diacylglycerollipase, and acyltransferase activities in vitro
Robert S. Munford,J P Hunter +1 more
TL;DR: The demonstration that AOAH has phospholipase, lysophospholipases, diacylglycerol lipase, and acyltransferase activities in vitro suggests that the enzyme may have roles in addition to LPS deacylation (detoxification) in phagocytic cells.
Journal ArticleDOI
Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme.
Andrea Scaloni,W.M. Jones,Donatella Barra,M Pospischil,S Sassa,A Popowicz,L.R. Manning,Olaf Schneewind,James M. Manning +8 more
TL;DR: Ebelactone A, an inhibitor of the formyl aminopeptidase, the bacterial counterpart of eukaryotic acylpeptide hydrolase, was found to be an effective inhibitor of this enzyme.
Journal ArticleDOI
Evidence of a Double-Lid Movement in Pseudomonas aeruginosa Lipase: Insights from Molecular Dynamics Simulations
Subbulakshmi Latha Cherukuvada,Aswin Sai Narain Seshasayee,Krishnan Raghunathan,Sharmila Anishetty,Gautam Pennathur,Gautam Pennathur +5 more
TL;DR: It is proposed that there exists, in addition to the above-mentioned lid, a novel second lid in this lipase, and it is shown that the second lid, covering residues 210–222, acts as a triggering lid for the movement of the first.
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.