Alterations in kinetic properties of penicillin-binding proteins of penicillin-resistant Streptococcus pneumoniae. Academic Article uri icon

Overview

abstract

  • Earlier studies have shown that the highly penicillin-resistant South African Strains of pneumococci contain altered penicillin-binding proteins (PBPs) (S. Zighelboim and A. Tomasz, Antimicrob. Agents Chemother. 17:434-442, 1980). We now describe a detailed quantitative characterization of the reaction of radioactively labeled penicillin with the PBPs of the penicillin-susceptible and penicillin-resistant pneumococci and several intermediate-resistance-level genetic transformants as well. The altered binding of the antibiotic by the PBPs of resistant cells appears to be due to a combination of two factors: lower drug affinity and change in the cellular amounts of PBPs. No alteration in the rates of deacylation of the penicilloyl-PBPs of the resistant cells was detected.

publication date

  • July 1, 1986

Research

keywords

  • Bacterial Proteins
  • Carboxypeptidases
  • Carrier Proteins
  • Hexosyltransferases
  • Muramoylpentapeptide Carboxypeptidase
  • Penicillins
  • Peptidyl Transferases
  • Streptococcus pneumoniae

Identity

PubMed Central ID

  • PMC176435

Scopus Document Identifier

  • 0022642829

PubMed ID

  • 3638932

Additional Document Info

volume

  • 30

issue

  • 1