Literature DB >> 6334067

The affinity of imipenem (N-formimidoylthienamycin) for the penicillin-binding proteins of Staphylococcus aureus--binding and release.

T Hashizume, W Park, M Matsuhashi.   

Abstract

Penicillin-binding proteins 1, 2 and 3 in Staphylococcus aureus were found to possess common properties. All have very strong affinities for both benzylpenicillin and imipenem (N-formimidoylthienamycin), and all have an activity which releases bound imipenem, but not bound benzylpenicillin. Lower molecular weight penicillin-binding protein 4, which has a rather weak affinity for benzylpenicillin and also weak penicillinase activity showed an extraordinarily high affinity for imipenem but no antibiotic-releasing activity.

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Year:  1984        PMID: 6334067     DOI: 10.7164/antibiotics.37.1049

Source DB:  PubMed          Journal:  J Antibiot (Tokyo)        ISSN: 0021-8820            Impact factor:   2.649


  3 in total

Review 1.  Imipenem/cilastatin. A review of its antibacterial activity, pharmacokinetic properties and therapeutic efficacy.

Authors:  S P Clissold; P A Todd; D M Campoli-Richards
Journal:  Drugs       Date:  1987-03       Impact factor: 9.546

2.  Molecular cloning of the gene of a penicillin-binding protein supposed to cause high resistance to beta-lactam antibiotics in Staphylococcus aureus.

Authors:  M Matsuhashi; M D Song; F Ishino; M Wachi; M Doi; M Inoue; K Ubukata; N Yamashita; M Konno
Journal:  J Bacteriol       Date:  1986-09       Impact factor: 3.490

3.  Autolysis of methicillin-resistant Staphylococcus aureus is involved in synergism between imipenem and cefotiam.

Authors:  K Matsuda; K Nakamura; Y Adachi; M Inoue; M Kawakami
Journal:  Antimicrob Agents Chemother       Date:  1995-12       Impact factor: 5.191

  3 in total

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