Interaction of nocardicin A with the penicillin-binding proteins of Escherichia coli in intact cells and in purified cell envelopes.
This study deals with the interaction of nocardicin A with Escherichia coli penicillin-binding proteins. Competition experiments with two different isotopically labelled beta-lactams indicated that nocardicin A interacts with penicillin-binding proteins 1a, 1b, 2 and 4 in intact cells. Binding of nocardicin A to the penicillin-binding proteins was abolished, or greatly reduced, when the assays were carried out with purified cell envelopes. Important differences between the binding patterns of benzyl[14C]penicillin to intact cells and to purified cell envelopes were also observed. These results suggest that the interaction of beta-lactam antibiotics with their target proteins depends to a very great extent on the state of the cell envelope as a whole.
D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D006602:Hexosyltransferases; D007769:Lactams; D002267:Muramoylpentapeptide Carboxypeptidase; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D011485:Protein Binding
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; C027318:nocardicin; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase