JBC, Vol. 251, Issue 17, 5361-5365, Sep, 1976
Deacetylation reaction catalyzed by Salmonella phage c341 and its baseplate parts
S. Iwashita and S. Kanegasaki
Phage c341 was shown to cleave off 14C-acetyl groups from a 14C-acetylated
polysaccharide, prepared by the enzymatic acetylation of alkali-treated
Salmonella anatum O-polysaccharide catalyzed by a membrane fraction from S.
anatum (O-10 transacetylase). No deacetylation reaction was detected if the
substate was prepared from alkali-treated O-polysaccharide of Salmonella
newington. The structural difference of these O-polysaccharides is the
anomeric configuration of the linkage between the common
mannosyl-rhamnosyl-galactose repeating units. A soluble protein obtained
from phage c341 lysate, which has previously been identified as the free
form of the baseplate parts of this phage, showed the deacetylase activity,
a result indicating that the baseplate is responsible for the enzymatic
activity of the phage particles. These results suggest that as in the case
of other Salmonella phages such as epsilon15, epsilon34, and P22 that
contain glycosidases as baseplates, the baseplate deacetylase of c341 plays
a role for phage adsorption through the formation of enzyme-substrate type
complexes with the receptor O-polysaccharide.
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