PMID: 9532794Apr 9, 1998Paper

Molecular properties and activity of amino-terminal truncated forms of lipase activator protein

Bioscience, Biotechnology, and Biochemistry
H ShibataJ Oda

Abstract

Two mutant forms, which had truncated N-terminals, of lipase activator protein (LipB) from Pseudomonas aeruginosa TE3285 were prepared, and their molecular properties and activity were compared with those of the full-length form. A truncated LipB lacking its hydrophobic N-terminal 21 residues was dispersed homogeneously in solution, and could reactivate the stoichiometric amount of denatured lipase. In contrast, full-length LipB formed soluble aggregates, and reactivated less than an equimolar amount of the lipase even under the most suitable conditions. These findings suggest that some or all of the N-terminal 21 residues caused aggregation of the protein molecules, and prevented LipB from fully stoichiometric reactivation. A truncated LipB lacking the N-terminal 61 residues also reactivated denatured lipase, suggesting that the N-terminal 61-residue region of LipB is not involved in reactivation.

References

Jan 1, 1976·Analytical Biochemistry·A Bensadoun, D Weinstein
Aug 1, 1992·Archives of Biochemistry and Biophysics·M Chihara-SiomiJ Oda
Jun 15, 1993·Proceedings of the National Academy of Sciences of the United States of America·A H HobsonD J McConnell
Aug 1, 1993·Molecular Microbiology·L G FrenkenC T Verrips

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Citations

Jul 28, 2007·Extremophiles : Life Under Extreme Conditions·Hiroyasu OginoHaruo Ishikawa
Nov 17, 2012·International Journal of Biological Macromolecules·Xiaomei ZhengYunliu Fan
May 16, 2007·Molecular Microbiology·Kris PauwelsPatrick Van Gelder
Mar 7, 2006·Nature Structural & Molecular Biology·Kris PauwelsPatrick Van Gelder
Feb 5, 2004·Chembiochem : a European Journal of Chemical Biology·Frank RosenauKarl-Erich Jaeger

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