Identification of a group of Haemophilus influenzae penicillin-binding proteins that may have complementary physiological roles

Antimicrob Agents Chemother. 1990 Feb;34(2):363-5. doi: 10.1128/AAC.34.2.363.

Abstract

[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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Carrier Proteins / metabolism*
  • Carrier Proteins / physiology
  • Culture Media
  • Haemophilus influenzae / metabolism*
  • Hexosyltransferases*
  • Muramoylpentapeptide Carboxypeptidase / metabolism*
  • Muramoylpentapeptide Carboxypeptidase / physiology
  • Penicillin G / metabolism
  • Penicillin-Binding Proteins
  • Penicillins / metabolism*
  • Peptidyl Transferases*
  • Spectrometry, Fluorescence
  • Sulfur Radioisotopes
  • Temperature

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Culture Media
  • Penicillin-Binding Proteins
  • Penicillins
  • Sulfur Radioisotopes
  • Peptidyl Transferases
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • Penicillin G