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 language | English |
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Pages (from-to) | 1369-1374 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 582 |
Issue number | 9 |
DOIs | |
State | Published - Apr 16 2008 |
Externally published | Yes |
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