A murein hydrolase is the specific target of bulgecin in Escherichia coli

Markus F. Templin, David H. Edwards, Joachim-Volker Holtje

    Research output: Contribution to journalArticle

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    Abstract

    A deletion in the structural gene for the soluble lytic transglycosylase, the predominant murein hydrolase in the soluble fraction of Escherichia coli, has been constructed. The mutant grows normally but exhibits increased sensitivity toward mecillinam, a beta-lactam specific for penicillin-binding protein 2. In the presence of furazlocillin or other beta-lactams with a specificity for penicillin-binding protein 3 which normally cause filamentation, bulges were formed prior to rapid bacteriolysis. Similar morphological alterations are known to develop in wild type E. coli cells when furazlocillin is combined with bulgecin, an antibiotic of unusual glucosaminyl structure. It turned out that bulgecin specifically inhibits the Sl-transglycosylase in a noncompetitive manner. Since bulgecin shows some structural analogy to the murein subunits we postulate that the soluble lytic transglycosylase, in addition to its active site, has a recognition site for specific murein structures. The possibility of an allosteric modulation of the activity of the enzyme by changes in the structure of the murein sacculus is discussed.
    Original languageEnglish
    Pages (from-to)20039-20043
    Number of pages5
    JournalJournal of Biological Chemistry
    Volume267
    Issue number28
    Publication statusPublished - 5 Oct 1992

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    N-Acetylmuramoyl-L-alanine Amidase
    Peptidoglycan
    Escherichia coli
    Penicillin-Binding Proteins
    beta-Lactams
    Bacteriolysis
    Amdinocillin
    Catalytic Domain
    Genes
    Modulation
    Anti-Bacterial Agents
    Enzymes
    bulgecin
    murein transglycosylase
    furazlocillin

    Cite this

    Templin, Markus F. ; Edwards, David H. ; Holtje, Joachim-Volker. / A murein hydrolase is the specific target of bulgecin in Escherichia coli. In: Journal of Biological Chemistry. 1992 ; Vol. 267, No. 28. pp. 20039-20043.
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    abstract = "A deletion in the structural gene for the soluble lytic transglycosylase, the predominant murein hydrolase in the soluble fraction of Escherichia coli, has been constructed. The mutant grows normally but exhibits increased sensitivity toward mecillinam, a beta-lactam specific for penicillin-binding protein 2. In the presence of furazlocillin or other beta-lactams with a specificity for penicillin-binding protein 3 which normally cause filamentation, bulges were formed prior to rapid bacteriolysis. Similar morphological alterations are known to develop in wild type E. coli cells when furazlocillin is combined with bulgecin, an antibiotic of unusual glucosaminyl structure. It turned out that bulgecin specifically inhibits the Sl-transglycosylase in a noncompetitive manner. Since bulgecin shows some structural analogy to the murein subunits we postulate that the soluble lytic transglycosylase, in addition to its active site, has a recognition site for specific murein structures. The possibility of an allosteric modulation of the activity of the enzyme by changes in the structure of the murein sacculus is discussed.",
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    A murein hydrolase is the specific target of bulgecin in Escherichia coli. / Templin, Markus F.; Edwards, David H.; Holtje, Joachim-Volker.

    In: Journal of Biological Chemistry, Vol. 267, No. 28, 05.10.1992, p. 20039-20043.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - A murein hydrolase is the specific target of bulgecin in Escherichia coli

    AU - Templin, Markus F.

    AU - Edwards, David H.

    AU - Holtje, Joachim-Volker

    PY - 1992/10/5

    Y1 - 1992/10/5

    N2 - A deletion in the structural gene for the soluble lytic transglycosylase, the predominant murein hydrolase in the soluble fraction of Escherichia coli, has been constructed. The mutant grows normally but exhibits increased sensitivity toward mecillinam, a beta-lactam specific for penicillin-binding protein 2. In the presence of furazlocillin or other beta-lactams with a specificity for penicillin-binding protein 3 which normally cause filamentation, bulges were formed prior to rapid bacteriolysis. Similar morphological alterations are known to develop in wild type E. coli cells when furazlocillin is combined with bulgecin, an antibiotic of unusual glucosaminyl structure. It turned out that bulgecin specifically inhibits the Sl-transglycosylase in a noncompetitive manner. Since bulgecin shows some structural analogy to the murein subunits we postulate that the soluble lytic transglycosylase, in addition to its active site, has a recognition site for specific murein structures. The possibility of an allosteric modulation of the activity of the enzyme by changes in the structure of the murein sacculus is discussed.

    AB - A deletion in the structural gene for the soluble lytic transglycosylase, the predominant murein hydrolase in the soluble fraction of Escherichia coli, has been constructed. The mutant grows normally but exhibits increased sensitivity toward mecillinam, a beta-lactam specific for penicillin-binding protein 2. In the presence of furazlocillin or other beta-lactams with a specificity for penicillin-binding protein 3 which normally cause filamentation, bulges were formed prior to rapid bacteriolysis. Similar morphological alterations are known to develop in wild type E. coli cells when furazlocillin is combined with bulgecin, an antibiotic of unusual glucosaminyl structure. It turned out that bulgecin specifically inhibits the Sl-transglycosylase in a noncompetitive manner. Since bulgecin shows some structural analogy to the murein subunits we postulate that the soluble lytic transglycosylase, in addition to its active site, has a recognition site for specific murein structures. The possibility of an allosteric modulation of the activity of the enzyme by changes in the structure of the murein sacculus is discussed.

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    VL - 267

    SP - 20039

    EP - 20043

    JO - Journal of Biological Chemistry

    JF - Journal of Biological Chemistry

    SN - 0021-9258

    IS - 28

    ER -