An Escherichia coli expression system for glutamyl endopeptidases optimized by complete suppression of autodegradation
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An Escherichia coli expression system for glutamyl endopeptidases optimized by complete suppression of autodegradation.
V8 protease (GluV8), a member of the glutamyl endopeptidase I family isolated from the V8 strain of Staphylococcus aureus, is widely used for proteome analysis because of its unique substrate specificity and resistance to detergents. We recently developed an Escherichia coli expression system for the production of GluV8 based on a technique that suppresses the autoproteolysis--the use of the pr...
متن کاملTitle An Escherichia coli expression system for glutamyl endopeptidasesoptimized by complete suppression of autodegradation
Title An Escherichia coli expression system for glutamyl endopeptidases optimized by complete suppression of autodegradation Author(s) Ono, Toshio; Nemoto, Takayuki K; Shimoyama, Yu; Kimura, Shigenobu; Ohara-Nemoto, Yuko Citation Analytical Biochemistry, 381(1), pp.74-80; 2008 Issue Date 2008-10-01 URL http://hdl.handle.net/10069/19225 Right Copyright (c) 2008 Elsevier Inc. All rights reserved....
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15 صفحه اولGlutamyl Endopeptidases: The Puzzle of Substrate Specificity
Glutamyl endopeptidases (GEPases) are chymotrypsin-like enzymes that preferentially cleave the peptide bonds of the α-carboxyl groups of glutamic acid. Despite the many years of research, the structural determinants underlying the strong substrate specificity of GEPases still remain unclear. In this review, data concerning the molecular mechanisms that determine the substrate preference of GEPa...
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ژورنال
عنوان ژورنال: Analytical Biochemistry
سال: 2008
ISSN: 0003-2697
DOI: 10.1016/j.ab.2008.06.022