Methanogens with pseudomurein use diaminopimelate aminotransferase in lysine biosynthesis

David E. Graham, Holly K. Huse

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

Methanothermobacter thermautotrophicus uses lysine for both protein synthesis and cross-linking pseudomurein in its cell wall. A diaminopimelate aminotransferase enzyme from this methanogen (MTH0052) converts tetrahydrodipicolinate to l,l-diaminopimelate, a lysine precursor. This gene complemented an Escherichia coli diaminopimelate auxotrophy, and the purified protein catalyzed the transamination of diaminopimelate to tetrahydrodipicolinate. Phylogenetic analysis indicated this gene was recruited from anaerobic Gram-positive bacteria. These results expand the family of diaminopimelate aminotransferases to a diverse set of plant, bacterial and archaeal homologs. In contrast marine methanogens from the Methanococcales, which lack pseudomurein, appear to use a different diaminopimelate pathway for lysine biosynthesis.

Original languageEnglish
Pages (from-to)1369-1374
Number of pages6
JournalFEBS Letters
Volume582
Issue number9
DOIs
StatePublished - Apr 16 2008
Externally publishedYes

Funding

This work was supported in part by grants from NIH (AI06444-01) and the Petroleum Research Foundation (44382-G4).

Keywords

  • Biosynthesis
  • Cell wall
  • Convergent evolution
  • Lysine
  • Methanogen

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