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A novel pathway of peptide biosynthesis found in methanogenic Archaea

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The peptide subunits of the pseudomurein, the cell-wall peptidoglycan of some methanogens, are usually composed of glutamic acid, alanine and lysine. In order to get a more detailed picture of the biosynthetic pathway of the peptide subunit, we performed in vitro assays. Starting from glutamic acid a pentapeptide was obtained in seven steps:

$$\begin{gathered} N^\alpha - UDP - Glu^\gamma \to Ala \to ^\varepsilon Lys \to Ala \hfill \\ \uparrow ^\gamma \hfill \\ Glu \hfill \\ \end{gathered} $$

The pentapeptide structure was identical to that of the peptide subunit of the intact pseudomurein except one additional alanine residue, which is split off during further processing. The pentapeptide synthesis starts with glutamic acid, which is phosphorylated at the Nα-amino group. Nα-phosphoryl-glutamic acid is transferred to a nucleotide-carrier, forming Nα-UDP-glutamic acid. The further tetrapeptide by stepwise addition of the corresponding amino acids.

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Correspondence to Evanmarie Hartmann.

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Hartmann, E., König, H. A novel pathway of peptide biosynthesis found in methanogenic Archaea. Arch. Microbiol. 162, 430–432 (1994).

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Key words

  • Methanogens
  • Archaea
  • Methanobacterium thermoautrophicum
  • Cell walls
  • Peptide biosynthesis
  • Pseudomurein