Purification of the peptidoglycan transglycosylase of Bacillus megaterium

A. Taku, M. Stuckey, D. P. Fan

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The peptidoglycan transglycosylase of B. megaterium has been purified approximately 500 fold from a crude membrane fraction. This protein is likely to be the one previously called PG-II and was assayed by its ability to reconstitute with a crude phospho-N-acetyl-muramyl-pentapeptide translocase preparation and partially purified N-acetylglucosaminyl transferase to give peptidoglycan synthesis from nucleotide precursors. The protein was identified as the peptidoglycan transglycosylase by its ability to synthesize lysozyme-sensitive peptidoglycan from undecaprenylpyrophosphoryl-disaccharide-pentapeptide. The enzyme is inhibited by vancomycin but not by bacitracin, penicillin G, or tunicamycin. The enzyme has no detectable transpeptidase activity, but it does bind penicillin.

Original languageEnglish (US)
Pages (from-to)5018-5022
Number of pages5
JournalJournal of Biological Chemistry
Issue number9
StatePublished - 1982


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