Reference : Modular Design of the Enterococcus Hirae Muramidase-2 and Streptococcus Faecalis Autolysin
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83770
Modular Design of the Enterococcus Hirae Muramidase-2 and Streptococcus Faecalis Autolysin
English
Joris, Bernard mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Englebert, Serge [Université de Liège - ULg > > Centre d'ingénierie des protéines > > > >]
Chu, Chien-Peng [Temple University School of Medecine - Philadelphia (USA) > Department of Microbiology and Immunology > > >]
Kariyama, Reiko [Temple University School of Medecine - Philadelphia (USA) > Department of Microbiology and Immunology > > > >]
Daneo-Moore, Lolita [Temple University School of Medecine - Philadelphia (USA) > Department of Microbiology and Immunology > > > >]
Shockman, Gerald D. [Temple University School of Medecine - Philadelphia (USA) > Department of Microbiology and Immunology > > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Departement de Chimie > Service de Microbiologie > > >]
15-Mar-1992
FEMS Microbiology Letters
Blackwell Publishing
91
3
257-264
Yes (verified by ORBi)
International
0378-1097
1574-6968
Oxford
United Kingdom
[en] Amino Acid Sequence ; Enterococcus/enzymology ; Enterococcus/genetics ; Enterococcus faecalis/enzymology ; Enterococcus faecalis/genetics ; Molecular Sequence Data ; Muramidase/genetics ; N-Acetylmuramoyl-L-alanine Amidase/genetics ; Protein Conformation ; Sequence Homology, Nucleic Acid
[en] The mature forms of the extracellular muramidase-2 of Enterococcus hirae and Streptococcus faecalis autolysin have very similar primary structures. Each consists of an active-site-containing N-terminal domain fused to a multiple-repeat C-terminal domain. Polypeptide segments occurring at equivalent places in these two bacterial wall lytic enzymes have homologues in two phage lysozymes and in three functionally unrelated proteins, illustrating the principle that protein molecules frequently are constructed from modules that are linked in a single polypeptide chain.
Centre d'Ingénierie des Protéines - CIP
Fonds de la Recherche Scientifique Médicale - FRSM ; Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS
Researchers ; Professionals
http://hdl.handle.net/2268/83770

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