Abstract

The endopeptidase(s) of ether-treated cells of Neisseria gonorrhoeae cleaved O-acetylated peptidoglycan dimers about 3 times as rapidly as non-O-acetylated dimers. This was true whether the enzyme came from a highly O-acetylated strain or from one with low O-acetylation. The penicillin-resistant fraction of the endopeptidase activity also showed the same substrate selectivity.

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