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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Permeability of the nuclear envelope at isolated Xenopus oocyte nuclei studied by scanning electrochemical microscopy.
Jidong Guo,Shigeru Amemiya +1 more
TL;DR: The result indicates that passive transport of the redox molecules across the NE is facilitated by open NPC pores, yielding the NE permeability to the molecules that is at least 2 orders of magnitude larger than permeability of bilayer lipid membranes and cell membranes.
Journal ArticleDOI
Production, regulation, and some properties of lipase activity from Fusarium oxysporum f. sp. vasinfectum
TL;DR: Lipase activity produced during cultivation of Fusarium oxysporum f.
Journal ArticleDOI
Characterization of the extracellular lipase, LipA, of Acinetobacter calcoaceticus BD413 and sequence analysis of the cloned structural gene
Ruben G. Kok,Jasper J. van Thor,Inge M. Nugteren-Roodzant,Marc B. W. Brouwer,Maarten R. Egmond,Clara B. Nudel,Ben Vosman,Klaas J. Hellingwerf +7 more
TL;DR: The extracellular lipase from Acinetobacter calcoaceticus BD413 was purified to homogeneity, via hydrophobic‐interaction fast performance liquid chromatography (FPLC), from cultures grown in mineral medium with hexadecane as the sole carbon source and shows high similarity to known lipases that are exported in a two‐step secretion mechanism and require a lipase‐specific chaperone.
Journal ArticleDOI
Biochemical and molecular characterization of Staphylococcus simulans lipase.
TL;DR: Staphylococcus simulans strain secretes a non-induced lipase in the culture medium, which is a tetrameric protein corresponding to the association of four lipase molecules and able to hydrolyze its substrate in the presence of bile salts or amphiphilic proteins.
Journal ArticleDOI
Identification of a second lipase gene, gehD, in Staphylococcus epidermidis: comparison of sequence with those of other staphylococcal lipases.
TL;DR: Construction of a phylogenetic tree and calculation of amino acid sequence homologies between mature lipases suggested that the lipases of S. epidermidis may be more closely related to those of Staphylococcus aureus than to each other.
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.