Penicillin-binding proteins and induction of AmpC beta-lactamase.
In competition assays for radiolabeled penicillin, penicillin-binding proteins (PBPs) 4, 7a, and 7b showed very high affinities for strong inducers of AmpC beta-lactamase. Loss of PBP 4 resulted in diminished inducibility. This suggests that if PBPs are involved in induction of AmpC beta-lactamase, there is probably a redundancy in function among the different PBPs.
Sanders
C C
CC
Center for Research in Anti-Infectives and Biotechnology, Department of Medical Microbiology, Creighton University School of Medicine, Omaha, Nebraska 68178, USA.
Bradford
P A
PA
Ehrhardt
A F
AF
Bush
K
K
Young
K D
KD
Henderson
T A
TA
Sanders
W E
WE
D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D004790:Enzyme Induction; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism*; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D001618:beta-Lactamases / Q000096:biosynthesis*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; C048795:AmpC beta-lactamases; D001618:beta-Lactamases