Affinities of SM-7338 for penicillin-binding proteins and its release from these proteins in Staphylococcus aureus

Yoshihiro Sumita, M. Fukasawa, T. Okuda

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

SM-7338, a carbapenem antibiotic, had high affinities for penicillin-binding proteins (PBPs) 1, 2, and 4 of Staphylococcus aureus but not for PBP 3 when a competition assay with [14C]benzylpenicillin was used. However, binding of [14C]SM-7338 was saturated for PBP 3 at a concentration of 1 μg/ml. These results were due to the rapid release of SM-7338 from PBP 3-SM-7338 complexes with a half-life of 2 min.

Original languageEnglish
Pages (from-to)484-486
Number of pages3
JournalAntimicrobial Agents and Chemotherapy
Volume34
Issue number3
DOIs
Publication statusPublished - Jan 1 1990
Externally publishedYes

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meropenem
Penicillin-Binding Proteins
Staphylococcus aureus
Proteins
Carbapenems
Penicillin G
Half-Life

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases

Cite this

Affinities of SM-7338 for penicillin-binding proteins and its release from these proteins in Staphylococcus aureus. / Sumita, Yoshihiro; Fukasawa, M.; Okuda, T.

In: Antimicrobial Agents and Chemotherapy, Vol. 34, No. 3, 01.01.1990, p. 484-486.

Research output: Contribution to journalArticle

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