type	Journal Article
authors	Graham DE, Huse HK.
title	Methanogens with pseudomurein use diaminopimelate aminotransferase in lysine biosynthesis
journal	FEBS Lett
Activity	2.6.1.83
Family	2.6.1.83.a
sel	selected
ui	18371309
year	(2008)
volume	3582
number	9
pages	1369-74
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.
last changed	2010/12/06 15:53