Structure of peptidoglycan from Thermus thermophilus HB8.

摘要: The composition and structure of peptidoglycan (murein) extracted from the extreme thermophilic eubacterium Thermus thermophilus HB8 are presented. 29 muropeptides, accounting for more than 85% total murein, is reported. basic monomeric subunit consists N-acetylglucosamine-N-acetylmuramic acid-L-Ala-D-Glu-L-Orn-D-Ala-D-Ala, acylated at delta-NH2 group Orn by a Gly-Gly dipeptide. In significant proportion (about 23%) N-terminal Gly substituted residue phenylacetic acid. This first time acid described as component bacterial murein. Possible implications murein physiology biosynthesis discussed. Murein cross-linking mediated D-Ala-Gly-Gly peptide cross-bridges. Glycan chains apparently terminated (1-->6) anhydro N-acetylmuramic residues. Neither reducing sugars nor murein-bound macromolecules were detected. T. presents an intermediate complexity between those gram-positive gram-negative organisms. cross-bridges typical bacterium. However, content, degree cross-linkage, glycan chain length closer to organisms could explain character spp.