Isolation of nucleotide activated amino acid and peptide precursors of the pseudomurein of Methanobacterium thermoautotrophicum.
The following putative precursors of the pseudomurein were isolated from trichloroacetic acid extracts of Methanobacterium thermoautotrophicum: a uridine diphosphate activated derivative of glutamic acid and the uridine diphosphate activated peptides (see text). The activated glutamic acid residue and the three activated pepetides lack the glycan components N-acetylglucosamine and N-acetyltalosaminuronic acid present in the intact pseudomurein. In this case uridine diphosphate should be directly linked to the amino group of a glutamic acid residue, which represents a new mode of amino acid and peptide activation.
Hartmann
E
E
Abteilung für Angewandte Mikrobiologie, Universität Ulm.
König
H
H
Kandler
O
O
Hammes
W
W
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D019605:Euryarchaeota / Q000032:analysis*; D005971:Glutamates; D018698:Glutamic Acid; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000032:analysis / Q000302:isolation & purification*; D010457:Peptidoglycan / Q000032:analysis* / Q000096:biosynthesis; D014530:Uridine Diphosphate
D005971:Glutamates; D009842:Oligopeptides; D010457:Peptidoglycan; D018698:Glutamic Acid; D014530:Uridine Diphosphate