Penicillin-binding proteins in Bacillus subtilis. The effects on penicillin-binding proteins and the antibacterial activities of .Beta.-lactams

Orikawa, S.; Ogawara, H.

The Journal of Antibiotics 33(6): 614-619

1980


DOI: 10.7164/antibiotics.33.614
Accession: 068515885

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Abstract
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.