Chemical composition of Eubacterium alactolyticum cell wall peptidoglycan.

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.

journal_name

Arch Microbiol

journal_title

Archives of microbiology

authors

Severin AI,Kokeguchi S,Kato K

doi

10.1007/BF00406563

subject

Has Abstract

pub_date

1989-01-01 00:00:00

pages

348-52

issue

4

eissn

0302-8933

issn

1432-072X

journal_volume

151

pub_type

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