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. 1983 Nov;156(2):649–655. doi: 10.1128/jb.156.2.649-655.1983

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

Z Markiewicz, B Glauner, U Schwarz
PMCID: PMC217879  PMID: 6630150

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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