Methanogens with pseudomurein use diaminopimelate aminotransferase in lysine biosynthesis
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.
Keywords: Lysine, Methanogen, Cell wall, Convergent evolution, Biosynthesis
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PII: S0014-5793(08)00250-0
doi:10.1016/j.febslet.2008.03.021
© 2008 Federation of European Biochemical Societies
