Penicillin-binding proteins in Bacteroides fragilis.
The penicillin binding proteins (PBSs) of Bacteroides fragilis, a clinically important Gram-negative rod, were studied. Four PBPs were detected by polyacrylamide gel electrophoresis/fluorography, PBP 4 (molecular weight, 35,000) being a minor PBP. The PBP pattern was thus different from that of the Enterobacteria and Pseudomonads. Antibacterial activity of beta-lactam antibiotics was associated with binding to PBP 1 (molecular weight, 100,000), 2 (molecular weight, 86,000) and 3 (molecular weight, 68,000). Binding to PBP 2 was associated with filamentation while binding to PBP 1 resulted in cell lysis.
D001426:Bacterial Proteins; D001441:Bacteroides fragilis / Q000378:metabolism*; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism*; D006602:Hexosyltransferases; D007700:Kinetics; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism*; D010458:Peptidyl Transferases; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G