Abstract
The structure of Eubacterium nodatum cell wall peptidoglycan was investigated. The peptide subunit of E. nodatum peptidoglycan has the following structure: L-Ala-D-Glu (Gly)-L-Orn-D-Ala. The carboxyl group of alanine occupying position 4 is attached to the δ-amino group of ornithine of an other subunit by the cross-linking bridge L-Ala-L-Ala-L-Orn. All glycine molecules are connected with the α-carboxyl group of glutamic acid with the ratio being 0.5-1. The hydrolysis of E. nodatum peptidoglycan by the S. albus G enzyme proceeds primarily due to the activity of alanyl-alanine endopeptidase, ornithyl-ornithine endopeptidase, ornithyl-alanine endopeptidase, N-acetyl-muramyl-alanine amidase, N-acetylmuramidase and N-acetylglucosaminidase.
Original language | English |
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Pages (from-to) | 353-358 |
Number of pages | 6 |
Journal | Archives of Microbiology |
Volume | 151 |
Issue number | 4 |
DOIs | |
Publication status | Published - Mar 1989 |
Keywords
- Eubacterium nodatum
- Lytic enzyme
- Peptidoglycan
ASJC Scopus subject areas
- Microbiology
- Biochemistry
- Molecular Biology
- Genetics