The amino acid sequence of the peptide subunits of the peptide moiety of the sacculus polymer (pseudomurein) of Methanobacterium thermoautotrophicum was elucidated by analysing overlapping peptides obtained from partial acid hydrolsates of isolated sacculi. It is suggested that the peptide subunits
N-Acetyltalosaminuronic acid a constituent of the pseudomurein of the genusMethanobacterium
✍ Scribed by Helmut König; Otto Kandler
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 478 KB
- Volume
- 123
- Category
- Article
- ISSN
- 0302-8933
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✦ Synopsis
By various chemical procedures including n i n h y d r i n -d e g r a d a t i o n it is shown that the as of yet u n k n o w n c o m p o u n d found in partial acid hydrolysates of isolated cell walls of Methanobacterium thermoautotrophicum and other species of this genus is 2-amino-2- deoxy-taluronic acid (N-Acetyltalosaminuronic acid) together with N-acetylglucosamine. It forms the glycan moiety o f pseudomurein.
📜 SIMILAR VOLUMES
Ristocetins A and B, elaborated by Nocardia lurida, 1 and related antibiotics are glycopeptides which inhibit cell wall biosynthesis in Gram positive bacteria by a mechanism involving complexation with peptide intermediates.2 The site of activity in the ristocetins has been shown to reside in the pe
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