Reference : Secretion by Overexpression and Purification of the Water-Soluble Streptomyces K15 Dd-Tr...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/82056
Secretion by Overexpression and Purification of the Water-Soluble Streptomyces K15 Dd-Transpeptidase/Penicillin-Binding Protein
English
Palomeque-Messia, Pilar [Université de Liège - ULg > Institut de Chimie > Centre d'Ingenierie des Proteines > >]
Quittre, Valérie [Université de Liège - ULg > Institut de Chimie > Centre d'Ingenierie des Proteines > >]
Leyh-Bouille, Mélina [Université de Liège - ULg > Institut de Chimie > Centre d'Ingenierie des Proteines > > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Gershater, Craig J. [SmithKline Beecham Pharmaceuticals > Department of Biotechnology > Biological Pilot Plant > >]
Dacey, Ian K. [SmithKline Beecham Pharmaceuticals > Department of Biotechnology > Biological Pilot Plant > >]
Dusart, Jean [Université de Liège - ULg > Institut de Chimie > Centre d'ingénieurie des Protéines > > >]
Van Beeumen, Jozef [Rijksuniversiteit-Gent > > Laboratorium voor Microbiologie en microbiële Genetica > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Centre d'ingénieurie des Protéines > > >]
15-Nov-1992
Biochemical Journal
Portland Press
288
1
87-91
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] Though synthesized with a cleavable signal peptide and devoid of membrane anchors, the 262-amino-acid-residue Streptomyces K15 DD-transpeptidase/penicillin-binding protein is membrane-bound. Overexpression in Streptomyces lividans resulted in the export of an appreciable amount of the synthesized protein (4 mg/litre of culture supernatant). The water-soluble enzyme was purified close to protein homogeneity with a yield of 75%. It requires the presence of 0.5 M-NaCl to remain soluble. It is indistinguishable from the detergent-extract wild-type enzyme with respect to molecular mass, thermostability, transpeptidase activity and penicillin-binding capacity.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/82056

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