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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Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein.
T J Chambers,R C Weir,Arash Grakoui,David W. McCourt,J F Bazan,Robert J. Fletterick,Charles M. Rice +6 more
TL;DR: To examine the putative proteolytic activity of NS3, segments of the yellow fever virus genome were subcloned into plasmid transcription/translation vectors and cell-free translation products were characterized and results suggest that a protease activity encoded within NS2B and the N-terminal one-third ofyellow fever virus NS3 is capable of cis-acting site-specific proteolysis at the NS2 B-NS3 cleavage site and dilution-insensitive cleavage
Journal ArticleDOI
Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
TL;DR: The three-dimensional structure of a recombinant cutinase from F. solani pisi is reported, an α–β protein; the active site is composed of the triad Ser 120, His 188 and Asp 175, and the catalytic serine is not buried under surface loops, but is accessible to solvent.
Journal ArticleDOI
The in vivo and in vitro degradation behavior of poly(trimethylene carbonate)
TL;DR: It can be concluded that enzymatic degradation plays an important role in the surface erosion of PTMC in vivo.
Journal ArticleDOI
From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes.
TL;DR: This review highlights and summarizes various studies that have aimed to improve the biochemical properties of industrially significant enzymes.
Journal ArticleDOI
Production of specific‐structured triacylglycerols by lipase‐catalyzed reactions: a review
TL;DR: Encouraging products resulting from this regiospecificity are reviewed together with the critical evaluation of their reaction schemes, side reactions and by-products, sources of substrate oils and acyl donors, and production processes.
References
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Frances C. Bernstein,Thomas F. Koetzle,Graheme J. B. Williams,Edgar F. Meyer,Michael D. Brice,John R. Rodgers,O. Kennard,Takehiko Shimanouchi,Mitsuo Tasumi +8 more
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Journal ArticleDOI
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Journal ArticleDOI
A graphics model building and refinement system for macromolecules
TL;DR: A model building and refinement system is described for use with a Vector General 3400 display that has been used to assist in difference Fourier map interpretation at medium and high resolution, and to build a protein molecule into a multiple isomorphous replacement phased electron density map.
Book ChapterDOI
Stereochemically restrained refinement of macromolecular structures.
TL;DR: Some extensions of the current export versions of the programs that have been implemented or are envisioned are described, expected to be important in realizing the goal of producing refined structural models that reproduce the diffraction patterns to within the accuracy of the measured data and which are compatible with prior stereochemical knowledge of macromolecules.
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.