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Journal Article

Novel type of murein transglycosylase in Escherichia coli

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Höltje,  JV
Schwarz Group, Friedrich Miescher Laboratory, Max Planck Society;

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Schwarz,  U
Schwarz Group, Friedrich Miescher Laboratory, Max Planck Society;

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Citation

Höltje, J., Mirelman, D., Sharon, N., & Schwarz, U. (1975). Novel type of murein transglycosylase in Escherichia coli. Journal of Bacteriology, 124(3), 1067-1076. doi:10.1128/jb.124.3.1067-1076.1975.


Cite as: https://hdl.handle.net/21.11116/0000-000C-6D75-7
Abstract
The purification and properties of a novel type of murein transglycosylase from Escherichia coli are described. The purified enzyme appears as a single band on sodium dodecyl sulfate-polyacrylamide gels and has an apparent molecular weight of approximately 65,000 as estimated by gel filtration and gel electrophoresis. It degrades pure murein sacculi from E. coli almost completely into low-molecular-weight products. The two prominent muropeptide fragments in the digest are the disaccharide-tripeptide N-acetylglucosamine-N-acetylmuramic acid-L-alanine-D-iso-glutamic acid-meso-diaminopimelic acid and the corresponding disaccharide-tetrapeptide N-acetylglucosamine-N-acetylmuramic acid-L-alanine-D-iso-glutamic acid-meso-diaminopimelic acid-D-alanine. The unique feature of these compounds is that the disaccharide has no reducing end group and that the muramic acid residue possesses an internal 1 leads to 6 anhydro linkage. The new lytic enzyme is designated as a murein: murein transglycosylase. Its possible role in the rearrangement of murein during cell growth and division is discussed.