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J Bacteriol. 1983 November; 156(2): 649-655

Murein structure and lack of DD- and LD-carboxypeptidase activities in Caulobacter crescentus.

ABSTRACT

High-pressure liquid chromatography of a muramidase digest of murein sacculi from Caulobacter crescentus showed that the absence of D-alanine carboxypeptidase activity in the cells was reflected by a very high content of pentapeptide in the murein. Approximately half of the pentapeptide side chains were shown to contain glycine, which replaced D-alanine as the terminal amino acid.

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