Penicillin-binding proteins in Bacillus subtilis. The effects on penicillin-binding proteins and the antibacterial activities of beta-lactams.
Several beta-lactams were investigated on the affinity for the penicillin-binding proteins (PBPs) and the antibacterial activity in Bacillus subtilis. The beta-lactams such as ampicillin, PS-5, methicillin and SCE-963, which had high affinities for PBP-2 showed strong antibacterial activities and the beta-lactams such as cephamycin C, Y-G19Z-GG and Y-G19Z-G, which had high affinities for PBP-1 but low affinities for PBP-2, showed weak antibacterial activities. Clavulanic acid and nocardicin A, which had almost no affinities for all the PBPs detected, showed very low antibacterial activities. These results suggest that PBP-2 in Bacillus subtilis is the lethal target of these beta-lactam antibiotics.
D001412:Bacillus subtilis / Q000187:drug effects*; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000494:pharmacology*; D006602:Hexosyltransferases; D008826:Microbial Sensitivity Tests; D002267:Muramoylpentapeptide Carboxypeptidase; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism / Q000494:pharmacology*; D010458:Peptidyl Transferases; D047090:beta-Lactams / Q000494:pharmacology*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D047090:beta-Lactams; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase