[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.
Research Center/Unit :
CIP - Centre d'Ingénierie des Protéines - ULiège
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Joris, Bernard ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Englebert, Serge; Université de Liège - ULiège > 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 - ULiège > Departement de Chimie > Service de Microbiologie
Language :
English
Title :
Modular Design of the Enterococcus Hirae Muramidase-2 and Streptococcus Faecalis Autolysin
Publication date :
15 March 1992
Journal title :
FEMS Microbiology Letters
ISSN :
0378-1097
eISSN :
1574-6968
Publisher :
Blackwell Publishing, Oxford, United Kingdom
Volume :
91
Issue :
3
Pages :
257-264
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRSM - Fonds de la Recherche Scientifique Médicale [BE] F.R.S.-FNRS - Fonds de la Recherche Scientifique [BE]
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