Chemical composition of Eubacterium alactolyticum cell wall peptidoglycan

Anatoly I. Severin, Susumu Kokeguchi, Keijiro Kato

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The mechanism of lysis of Eubacterium alactolyticum cell walls by Streptomyces albus G enzyme was studied. The analysis of the peptide terminal groups and peptide subunits isolated from the cell wall digest, released during solubilization of the cell walls, revealed that lytic action of S. albus G enzyme was mainly due to D-alanyl-A2pm endopeptidase, N-acetylmuramyl-L-alanine amidase, N-acetylmuramidase and N-acetylglucosaminidase. E. alactolyticum cell wall peptidoglycan is composed mainly of glucosamine, muramic acid, D-glutamic acid, L- and D-alanine, meso-diaminopimelic acid and glycine. The peptide subunit consists of L-alanyl-D-glutamyl-meso-A2pm-D-alanine. D-Alanine is connected directly with the amino group of the meso-A2pm residue of another peptide subunit. All of the L-amino groups of meso-diaminopimelic acid are involved in cross-linking. The possible structure of the peptide moiety of E. alactolyticum cell wall peptidoglycan is presented.

Original languageEnglish
Pages (from-to)348-352
Number of pages5
JournalArchives of Microbiology
Volume151
Issue number4
DOIs
Publication statusPublished - Mar 1 1989

Keywords

  • Eubacterium alactolyticum
  • Lytic enzyme
  • Peptidoglycan

ASJC Scopus subject areas

  • Microbiology
  • Biochemistry
  • Molecular Biology
  • Genetics

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