Specific Binding of the Soluble Lytic Transglycosylase to the Murein Sacculus 
of Escherichia coli

Romeis, T; Höltje, J-V

doi:10.1007/978-1-4757-9359-8_27

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Specific Binding of the Soluble Lytic Transglycosylase to the Murein Sacculus of Escherichia coli

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Romeis, T
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Höltje, J-V
Department Biochemistry, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Romeis, T., & Höltje, J.-V. (1993). Specific Binding of the Soluble Lytic Transglycosylase to the Murein Sacculus of Escherichia coli. In M. Pedro, J.-V. Höltje, & W. Löffelhardt (Eds.), Bacterial Growth and Lysis: Metabolism and Structure of the Bacterial Sacculus (pp. 235-240). Boston, MA, USA: Springer.

Cite as: https://hdl.handle.net/21.11116/0000-000E-A4E4-7

Abstract

Murein hydrolases, which are ubiquitous among bacteria (Ghuysen, 1968), represent a class of potentially autolytic enzymes and hence must be controlled strictly. However, little is known about the cellular control mechanism (Höltje and Tuomanen, 1991). This is in contrast to the detailed knowledge of the biochemistry of the murein synthesizing enzymes and their specific inhibition by a wide range of antibiotics. Due to this lack of information we are still far from understanding how the typical bacteriolytic response to inhibitors of murein synthesis is triggered (Tomasz, 1979).