Open AccessThe penicillin‐binding proteins of Zymomonas mobilis Zm4
Author(s) -
Karibian D.,
Starka G.
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02181.x
Subject(s) - zymomonas mobilis , penicillin binding proteins , strain (injury) , chemistry , microbiology and biotechnology , escherichia coli , biochemistry , biology , fermentation , gene , ethanol fuel , anatomy
The penicillin‐binding proteins (PBPs) of Zymomonas mobilis strain Zm4 were studied. The strain had 3 PBPs with apparent M r s of 90 000, 60 000, and 44 000. PBP1 and PBP2 were half‐saturated by concentrations of benzylpenicillin similar to the minimum inhibitory concentration (MIC) required to prevent bacterial growth, showing that PBP1 and/or PBP2 is probably an essential murein polymerase. The PBPs had much less affinity for mecillinam, to which Z. mobilis was relatively resistant. The PBP pattern of Zm4 differed considerably from those of Escherichia coli, Pseudomonas aeruginosa, Pseudomonas paucimobilis and even Z. mobilis ssp. pomaceae .