Abstract
The penicillin-binding proteins (PBPs) of Zymomonas mobilis strain Zm4 were studied. The strain had 3 PBPs with apparent Mrs 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.
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