Identification of a group of Haemophilus influenzae penicillin-binding proteins that may have complementary physiological roles.
[35S]penicillin bound to different Haemophilus influenzae proteins in assays performed at 20, 37, or 42 degrees C. Penicillin-binding proteins 3a, 3b, 4, and 4' formed a group characterized by their affinity for moxalactam, cefotaxime, and piperacillin. Penicillin-binding protein 4' showed specific properties that may reflect its complementary role in septation.
Malouin
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Lilly Research Laboratories, Eli Lilly & Company, Indianapolis, Indiana 46285-0438.
Parr
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Bryan
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D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism* / Q000502:physiology; D003470:Culture Media; D006193:Haemophilus influenzae / Q000378:metabolism*; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism* / Q000502:physiology; D010400:Penicillin G / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism*; D010458:Peptidyl Transferases; D013050:Spectrometry, Fluorescence; D013462:Sulfur Radioisotopes; D013696:Temperature
D001426:Bacterial Proteins; D002352:Carrier Proteins; D003470:Culture Media; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D013462:Sulfur Radioisotopes; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G