Peptidase; Bacteria; Actinomycetes; Actinomycetales; Streptomycetaceae; Enzyme; Streptomyces; Column chromatography; Radiolabelling; N terminal-Sequence; Active site; Penicillin; Binding protein; Protéine de liaison; Bactérie; Chromatographie colonne; Marquage radioisotopique; Séquence N terminale; Site actif; Pénicilline; Proteina de enlace; Enzima; Cromatografía columna; Marcación radioisotópica; Secuencia N terminal; Lugar activo
Abstract :
[en] The N-terminal region of the Streptomyces K15 DD-peptidase/penicillin-binding protein shows high homology with that of other penicillin-interactive proteins or domains. The active-site serine residue of the conserved tetrad Ser-Xaa-Xaa-Lys occurs at position 35. There is no indication for the presence of a signal peptide or an N-terminal hydrophobic sequence, suggesting that the Streptomyces K15 enzyme is probably anchored to the membrane by a C-terminal peptide segment.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Leyh-Bouille, Mélina; Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie
Vanbeeumen, Jozef; Rijksuniversiteit-Gent > Laboratorium voor Microbiologie
Renier-Pirlot, Suzanne; Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie
Joris, Bernard ; Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie
Nguyen-Distèche, Martine ; Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie
Ghuysen, Jean-Marie ; Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie
Language :
English
Title :
The Streptomyces K15 DD-peptidase/penicillin-binding protein. Active site and sequence of the N-terminal region.
Publication date :
1989
Journal title :
Biochemical Journal
ISSN :
0264-6021
eISSN :
1470-8728
Publisher :
Portland Press, London, United Kingdom
Volume :
260
Issue :
2
Pages :
601-604
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
FRSM - Fonds de la Recherche Scientifique Médicale Fond de la Recherche de la Faculté de Médecine ULg
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