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Опубликовано
2008-01-01
Опубликовано на SciPeople2010-09-08 15:35:10
ЖурналBiochemical and Biophysical Research Communications
The structural peptidoglycan hydrolase gp181 of bacteriophage fi-KZ
Biochemical and Biophysical Research Communications 374 (2008) 747–751
Аннотация
Gp181 (2237 amino acids) of Pseudomonas aeruginosa bacteriophage uKZ (Myoviridae) is a structural virion
protein, which bears a peptidoglycan hydrolase domain near its C-terminus. This protein is supposed
to degrade the peptidoglycan locally during the infection process. Nine deletional mutants allowed delineation
of the peptidoglycan hydrolase domain between amino acids 1880–2042 (gp181M8) and analysis
of its biochemical properties. Gp181M8 tolerates a high ionic strength (>320 mM) and is less sensitive to
long thermal treatments compared to the similar uKZ endolysin. Gp181M8 lysed all tested outer membrane-
permeabilized Gram-negative species. The C-terminal distal end (amino acids 2043–2237)
enhances the specific activity of gp181M8 threefold, resulting in a twelve times higher activity than commercial
hen egg white lysozyme. These biochemical properties suggest that this novel peptidoglycan
hydrolase domain may be suitable for enzybiotic applications.
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